groes protein

Summary

Summary: A chaperonin 10 heat-shock protein isolated from Escherichia coli.

Top Publications

  1. ncbi Machinery of protein folding and unfolding
    Xiaodong Zhang
    Centre for Structural Biology, Department of Biological Sciences, Imperial College of Science, Technology and Medicine, Flowers Building, South Kensington, SW7 2AZ, London, UK
    Curr Opin Struct Biol 12:231-8. 2002
  2. pmc Native folding of aggregation-prone recombinant proteins in Escherichia coli by osmolytes, plasmid- or benzyl alcohol-overexpressed molecular chaperones
    Ario de Marco
    Protein Expression Unit, European Molecular Biology Laboratory, Heidelberg, Germany
    Cell Stress Chaperones 10:329-39. 2005
  3. ncbi Proteome-wide analysis of chaperonin-dependent protein folding in Escherichia coli
    Michael J Kerner
    Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18, D 82152 Martinsried, Germany
    Cell 122:209-20. 2005
  4. ncbi The disordered mobile loop of GroES folds into a defined beta-hairpin upon binding GroEL
    F Shewmaker
    Department of Biochemistry, Tulane University Health Sciences Center, New Orleans, Louisiana 70112-2699, USA
    J Biol Chem 276:31257-64. 2001
  5. pmc Translocation boost protein-folding efficiency of double-barreled chaperonins
    Ivan Coluzza
    Cambridge University Centre for Computational Chemistry, Department of Chemistry, Cambridge, United Kingdom
    Biophys J 90:3375-81. 2006
  6. ncbi Chaperonin-mediated protein folding: fate of substrate polypeptide
    Wayne A Fenton
    Department of Genetics, Yale University School of Medicine, 295 Congress Avenue, New Haven, CT 06510, USA
    Q Rev Biophys 36:229-56. 2003
  7. ncbi Molecular mechanisms of chaperonin GroEL-GroES function
    O Keskin
    Molecular Structure Section, Laboratory of Experimental and Computational Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892, USA
    Biochemistry 41:491-501. 2002
  8. ncbi Structural features of the GroEL-GroES nano-cage required for rapid folding of encapsulated protein
    Yun Chi Tang
    Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18, D 82152 Martinsried, Germany
    Cell 125:903-14. 2006
  9. pmc Role of the gamma-phosphate of ATP in triggering protein folding by GroEL-GroES: function, structure and energetics
    Charu Chaudhry
    Department of Molecular Biophysics and Biochemistry and Howard Hughes Medical Institute, Yale University, New Haven, CT, USA
    EMBO J 22:4877-87. 2003
  10. ncbi The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex
    Z Xu
    The Howard Hughes Medical Institute, The Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06510, USA
    Nature 388:741-50. 1997

Research Grants

  1. Chaperonin-mediated protein folding
    Arthur Horwich; Fiscal Year: 2007
  2. TARGETING OF HUMAN OTC TO THE MITOCHONDRIAL MATRIX
    Arthur Horwich; Fiscal Year: 1992
  3. GROEL-MEDIATED PROTEIN FOLDING
    Arthur Horwich; Fiscal Year: 2000
  4. MECHANISM OF ACTION OF THE HSP100 CHAPERONE CLPA
    Arthur Horwich; Fiscal Year: 2006
  5. FUNCTION OF GROEL IN THE BACTERIAL CYTOPLASM
    Arthur Horwich; Fiscal Year: 1993
  6. Structural Dynamics of Biomolecular Systems
    Ivet Bahar; Fiscal Year: 2009
  7. Bridging Sequence Patterns and Structural Dynamics
    Ivet Bahar; Fiscal Year: 2009
  8. Computational and experimental studies of targets of protein kinase inhibitors
    ADRIAN HAMILTON ELCOCK; Fiscal Year: 2010
  9. Bridging Sequence Patterns and Structural Dynamics
    Ivet Bahar; Fiscal Year: 2010
  10. Structural Dynamics of Biomolecular Systems
    Ivet Bahar; Fiscal Year: 2010

Scientific Experts

Detail Information

Publications118 found, 100 shown here

  1. ncbi Machinery of protein folding and unfolding
    Xiaodong Zhang
    Centre for Structural Biology, Department of Biological Sciences, Imperial College of Science, Technology and Medicine, Flowers Building, South Kensington, SW7 2AZ, London, UK
    Curr Opin Struct Biol 12:231-8. 2002
    ..The majority of folding/unfolding machines adopt oligomeric ring structures in a cooperative fashion and utilise the conformational changes induced by ATP binding/hydrolysis for their specific functions...
  2. pmc Native folding of aggregation-prone recombinant proteins in Escherichia coli by osmolytes, plasmid- or benzyl alcohol-overexpressed molecular chaperones
    Ario de Marco
    Protein Expression Unit, European Molecular Biology Laboratory, Heidelberg, Germany
    Cell Stress Chaperones 10:329-39. 2005
    ....
  3. ncbi Proteome-wide analysis of chaperonin-dependent protein folding in Escherichia coli
    Michael J Kerner
    Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18, D 82152 Martinsried, Germany
    Cell 122:209-20. 2005
    ..We suggest that the chaperonin system may have facilitated the evolution of this fold into a versatile platform for the implementation of numerous enzymatic functions...
  4. ncbi The disordered mobile loop of GroES folds into a defined beta-hairpin upon binding GroEL
    F Shewmaker
    Department of Biochemistry, Tulane University Health Sciences Center, New Orleans, Louisiana 70112-2699, USA
    J Biol Chem 276:31257-64. 2001
    ..Analysis of sequence conservation suggests that sequences of the mobile loop and strongly binding peptide were selected for the ability to adopt this hairpin conformation...
  5. pmc Translocation boost protein-folding efficiency of double-barreled chaperonins
    Ivan Coluzza
    Cambridge University Centre for Computational Chemistry, Department of Chemistry, Cambridge, United Kingdom
    Biophys J 90:3375-81. 2006
    ..Moreover, we argue that internal folding is both more efficient and safer than a scenario where partially refolded proteins escape from the complex before being recaptured...
  6. ncbi Chaperonin-mediated protein folding: fate of substrate polypeptide
    Wayne A Fenton
    Department of Genetics, Yale University School of Medicine, 295 Congress Avenue, New Haven, CT 06510, USA
    Q Rev Biophys 36:229-56. 2003
    ....
  7. ncbi Molecular mechanisms of chaperonin GroEL-GroES function
    O Keskin
    Molecular Structure Section, Laboratory of Experimental and Computational Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892, USA
    Biochemistry 41:491-501. 2002
    ..These modes of motion could be used to manipulate the substrate's conformations...
  8. ncbi Structural features of the GroEL-GroES nano-cage required for rapid folding of encapsulated protein
    Yun Chi Tang
    Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18, D 82152 Martinsried, Germany
    Cell 125:903-14. 2006
    ..We suggest that by combining these features, the chaperonin cage provides a physical environment optimized to catalyze the structural annealing of proteins with kinetically complex folding pathways...
  9. pmc Role of the gamma-phosphate of ATP in triggering protein folding by GroEL-GroES: function, structure and energetics
    Charu Chaudhry
    Department of Molecular Biophysics and Biochemistry and Howard Hughes Medical Institute, Yale University, New Haven, CT, USA
    EMBO J 22:4877-87. 2003
    ..We discuss the likely basis of the ability of gamma-phosphate binding to convert preformed GroEL-GroES-ADP-polypeptide complexes into the folding-active state...
  10. ncbi The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex
    Z Xu
    The Howard Hughes Medical Institute, The Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06510, USA
    Nature 388:741-50. 1997
    ..When combined with new functional results, this negative allosteric mechanism suggests a model for an ATP-driven folding cycle that requires a double toroid...
  11. ncbi Residues in chaperonin GroEL required for polypeptide binding and release
    W A Fenton
    Department of Genetics, Yale University School of Medicine, Boyer Center, New Haven, Connecticut 06510
    Nature 371:614-9. 1994
    ..A highly conserved residue, Asp 87, positioned within a putative nucleotide-binding pocket in the top of the equatorial domain, is essential for ATP hydrolysis and polypeptide release...
  12. pmc A mobile loop order-disorder transition modulates the speed of chaperonin cycling
    Frank Shewmaker
    Department of Biochemistry, Tulane University Health Sciences Center, New Orleans, Louisiana 70112, USA
    Protein Sci 13:2139-48. 2004
    ..Thus, the free energy of mobile-loop ordering and disordering acts like the inertia of an engine's flywheel by modulating the speed of chaperonin conformational changes...
  13. ncbi Directed evolution of substrate-optimized GroEL/S chaperonins
    Jue D Wang
    Howard Hughes Medical Institute and Department of Cellular and Molecular Pharmacology, University of California, San Francisco 94143, USA
    Cell 111:1027-39. 2002
    ..This conflict and the nature of the ring structure may help explain the evolution of cellular chaperone systems...
  14. ncbi Mapping pathways of allosteric communication in GroEL by analysis of correlated mutations
    Itamar Kass
    Department of Structural Biology, Weizmann Institute of Science, Rehovot, Israel
    Proteins 48:611-7. 2002
    ..The results are discussed in the context of available structural, genetic, and biochemical data concerning short- and long-range interactions in the GroE system...
  15. ncbi The importance of a mobile loop in regulating chaperonin/ co-chaperonin interaction: humans versus Escherichia coli
    A Richardson
    Departement de Biochimie Medicale, Centre Medical Universitaire, 1 rue Michel Servet, 1211 Geneva, Switzerland
    J Biol Chem 276:4981-7. 2001
    ..It seems likely that the single ring mitochondrial Hsp60 exhibits intrinsically lower affinity for the co-chaperonin that can be compensated for by a higher affinity mobile loop...
  16. pmc Bacteriophage-encoded cochaperonins can substitute for Escherichia coli's essential GroES protein
    France Keppel
    Departement de Biochimie Medicale, Centre Medicale Universitaire, Geneva, Switzerland
    EMBO Rep 3:893-8. 2002
    ..Thus, it appears that, despite very little sequence identity with groES, the bacteriophage-encoded Gp31 and CocO proteins are capable of replacing GroES in the folding of E. coli's essential, housekeeping proteins...
  17. ncbi A mutant chaperonin with rearranged inter-ring electrostatic contacts and temperature-sensitive dissociation
    B Trevor Sewell
    Electron Microscope Unit and Department of Chemistry, University of Cape Town, Rondebosch, South Africa
    Nat Struct Mol Biol 11:1128-33. 2004
    ..Lacking the allosteric signal from the opposite ring, these complexes cannot release their GroES and become trapped, dead-end states...
  18. ncbi Mechanisms of ATPases--a multi-disciplinary approach
    Mathieu Rappas
    Centre for Structural Biology, Department of Biological Sciences, Imperial College London, Flowers Building, South Kensington London SW7 2AZ, UK
    Curr Protein Pept Sci 5:89-105. 2004
    ..We will therefore discuss them in greater details in order to describe the wide range techniques being utilised...
  19. ncbi Exploring the structural dynamics of the E.coli chaperonin GroEL using translation-libration-screw crystallographic refinement of intermediate states
    Charu Chaudhry
    Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA
    J Mol Biol 342:229-45. 2004
    ....
  20. ncbi DnaK and DnaJ facilitated the folding process and reduced inclusion body formation of magnesium transporter CorA overexpressed in Escherichia coli
    Yong Chen
    Skirball Institute of Biomolecular Medicine and Department of Cell Biology, New York University School of Medicine, 540 First Avenue, New York, NY 10016, USA
    Protein Expr Purif 32:221-31. 2003
    ..These co-expression systems can be used for producing other membrane proteins in large quantities...
  21. ncbi Low temperature or GroEL/ES overproduction permits growth of Escherichia coli cells lacking trigger factor and DnaK
    S Vorderwülbecke
    Ciphergen Biosystems GmbH, Hannah Vogt Str 1, 37085 Göttingen, Germany
    FEBS Lett 559:181-7. 2004
    ..GroEL/GroES thus influences the folding of proteins previously identified as DnaK/TF substrates...
  22. ncbi Functional characterization of an archaeal GroEL/GroES chaperonin system: significance of substrate encapsulation
    Luis Figueiredo
    Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18a, D 82152 Martinsried, Germany
    J Biol Chem 279:1090-9. 2004
    ..Additionally, the release of only the folded protein from the GroEL/GroES cage may prevent adverse interactions of the GroEL substrates with the thermosome, which is not normally located within the same compartment...
  23. ncbi The architecture of the GroEL-GroES-(ADP)(7) chaperonin complex. II. Heptagrammal characterization of the folding
    A Janner
    Institute for Theoretical Physics, University of Nijmegen, Toernooiveld, 6525 ED Nijmegen, The Netherlands
    Acta Crystallogr D Biol Crystallogr 59:795-808. 2003
    ..The geometric and algebraic restrictions imposed on the indexed positions and on their structural relations by the integrality condition are presented in an appendix...
  24. ncbi Discrimination of ATP, ADP, and AMPPNP by chaperonin GroEL: hexokinase treatment revealed the exclusive role of ATP
    Fumihiro Motojima
    Chemical Resources Laboratory, Tokyo Institute of Technology, 4259 Nagatsuta, Midori ku, Yokohama 226 8503, Japan
    J Biol Chem 278:26648-54. 2003
    ..In the absence of hexokinase, apparent cis folding of rhodanese and malate dehydrogenase was observed in ADP and AMPPNP. Thus, the exclusive role of ATP in generation of the cis ternary complex is now evident...
  25. ncbi Interaction of GroEL and GroEL/GroES complexes with a nonnative subtilisin variant: a small-angle neutron scattering study
    Susan Krueger
    NIST Center for Neutron Research, National Institute of Standards and Technology, 100 Bureau Drive, Stop 8562, Bldg 235 Room E151, Gaithersburg, MD 20899 8562, USA
    J Struct Biol 141:240-58. 2003
    ..However, dPJ9 assumed a more symmetric shape when bound in the GroEL/GroES/dPJ9 complex with ATP. This important observation reflects the relative ability of ATP to promote refolding of protein substrates relative to that of ADP...
  26. ncbi Molecular chaperones--cellular machines for protein folding
    Stefan Walter
    Institut fur Organische Chemie and Biochemie, Technische Universitat Munchen, Lichtenbergstr 4, 85747 Garching, Deutschland
    Angew Chem Int Ed Engl 41:1098-113. 2002
    ..In this review, we discuss the principal features of this peculiar class of proteins, their structure-function relationships, and the underlying molecular mechanisms...
  27. ncbi Encapsulation of an 86-kDa assembly intermediate inside the cavities of GroEL and its single-ring variant SR1 by GroES
    Jiu Li Song
    Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas 75390, USA
    J Biol Chem 278:2515-21. 2003
    ....
  28. ncbi Expression, purification, and characterization of a novel recombinant fusion protein, rhTPO/SCF, in Escherichia coli
    Yuhui Zang
    State Key Laboratory of Pharmaceutical Biotechnology, School of Life Science, Nanjing University, PR China
    Protein Expr Purif 47:427-33. 2006
    ..Western blot analysis confirmed the identity of the purified protein. rhTPO/SCF stimulated a dose-dependent cell proliferation in both TF1 and Mo7e cell lines...
  29. pmc Error-prone DNA polymerase IV is regulated by the heat shock chaperone GroE in Escherichia coli
    Jill C Layton
    Department of Biology, Indiana University, Jordan Hall, 1001 East Third St, Bloomington, IN 47405, USA
    J Bacteriol 187:449-57. 2005
    ..We were unable to show that GroE interacts directly with Pol IV, suggesting that GroE may act indirectly. Together with previous results, these findings indicate that Pol IV is a component of several cellular stress responses...
  30. pmc Factors governing the substrate recognition by GroEL chaperone: a sequence correlation approach
    Tapan K Chaudhuri
    Department of Biochemical Engineering and Biotechnology, Indian Institute of Technology Delhi, Hauz Khas, New Delhi 110016, India
    Cell Stress Chaperones 10:24-36. 2005
    ....
  31. doi Determination of the number of active GroES subunits in the fused heptamer GroES required for interactions with GroEL
    Tatsuya Nojima
    Chemical Resources Laboratory R1 7, Tokyo Institute of Technology, Yokohama, Japan
    J Biol Chem 283:18385-92. 2008
    ..These results indicate the presence of an intermediate GroEL/substrate/GroES complex in which the substrate and GroES bind to GroEL by sharing seven common binding sites...
  32. pmc Do chaperonins boost protein yields by accelerating folding or preventing aggregation?
    A I Jewett
    Department of Chemistry and Biochemistry, University of California, Santa Barbara, California, USA
    Biophys J 94:2987-93. 2008
    ....
  33. doi Comparison of refolding activities between nanogel artificial chaperone and GroEL systems
    Wakiko Asayama
    Institute of Biomaterials and Bioengineering, Tokyo Medical and Dental University 2 3 10, Kanda Surugadai, Chiyoda ku, Tokyo 101 0062, Japan
    Int J Biol Macromol 42:241-6. 2008
    ..In the nanogel-GFP system, about 90% of the intensity was recovered within 10 min. The half time (t(1/2)) for refolding in the CHP nanogel system (36 s) is almost equal to that of the natural chaperone GroEL-GroES system...
  34. doi Chaperone mediated solubilization of 69-kDa recombinant maltodextrin glucosidase in Escherichia coli
    S Paul
    Department of Biochemical Engineering and Biotechnology, Indian Institute of Technology Delhi, Hauz Khas, New Delhi, India
    J Appl Microbiol 104:35-41. 2008
    ..To investigate the factors affecting expression and solubilization of Escherichia coli maltodextrin glucosidase in E. coli...
  35. ncbi Effects of divalent cations on encapsulation and release in the GroEL-assisted folding
    Hiroshi Okuda
    Department of Applied Biological Chemistry, School of Agriculture, Kinki University, 3327 204, Nakamachi, Nara, 631 8505, Japan
    Biometals 20:903-10. 2007
    ..SDS-PAGE and gel filtration analyses revealed that cobalt, nickel and zinc ions permit the formation of stable substrate-GroEL-GroES cis-ternary complexes, but prevent the release of METF from GroEL...
  36. pmc Fast-scanning atomic force microscopy reveals the ATP/ADP-dependent conformational changes of GroEL
    Masatoshi Yokokawa
    Laboratory of Plasma Membrane and Nuclear Signaling, Kyoto University Graduate School of Biostudies, Kyoto, Japan
    EMBO J 25:4567-76. 2006
    ....
  37. ncbi Inclusion body anatomy and functioning of chaperone-mediated in vivo inclusion body disassembly during high-level recombinant protein production in Escherichia coli
    Ursula Rinas
    Biochemical Engineering Division, GBF German Research Center for Biotechnology, Mascheroder Weg 1, D 38124 Braunschweig, Germany
    J Biotechnol 127:244-57. 2007
    ....
  38. ncbi Co-expression of chaperonin GroEL/GroES enhances in vivo folding of yeast mitochondrial aconitase and alters the growth characteristics of Escherichia coli
    Parul Gupta
    Department of Biochemical Engineering and Biotechnology, Indian Institute of Technology, Delhi, Hauz Khas, New Delhi 110016, India
    Int J Biochem Cell Biol 38:1975-85. 2006
    ..Optimum in vivo folding of aconitase requires co-production of complete E. coli chaperonin machinery GroEL and GroES together...
  39. ncbi Elucidation of steps in the capture of a protein substrate for efficient encapsulation by GroE
    Matthew J Cliff
    Department of Biochemistry, University of Bristol, School of Medical Sciences, UK
    J Biol Chem 281:21266-75. 2006
    ..This ensures efficient encapsulation of the polypeptide within the GroEL central cavity underneath GroES...
  40. ncbi [Role of GroEL/GroES chaperonin system and Lon protease in regulation of expression Vibrio fischeri lux genes in Escherichia coli cells]
    I V Manukhov
    Mol Biol (Mosk) 40:277-83. 2006
    ..We suppose, that the GroEL/GroES chaperonin systems is required for the folding of LuxR into an active protein, and the LuxR is the target for the ATP-dependent serine Lon protease of E. coli...
  41. ncbi An expanded protein folding cage in the GroEL-gp31 complex
    Daniel K Clare
    School of Crystallography, Birkbeck College, University of London, Malet Street, London WC1E 7HX, UK
    J Mol Biol 358:905-11. 2006
    ..At 56 kDa, gp23 is close to the maximum size limit of a polypeptide that is thought to fit inside the GroEL-GroES folding cage...
  42. pmc Probing the sequence of conformationally induced polarity changes in the molecular chaperonin GroEL with fluorescence spectroscopy
    So Yeon Kim
    Department of Chemistry, Stanford University, Stanford, California 94305, USA
    J Phys Chem B 109:24517-25. 2005
    ....
  43. ncbi Leu309 plays a critical role in the encapsulation of substrate protein into the internal cavity of GroEL
    Ayumi Koike-Takeshita
    Chemical Resources Laboratory, Tokyo Institute of Technology, Midori ku, Yokohama, Japan
    J Biol Chem 281:962-7. 2006
    ..Thus, conformational communication between the two GroES contact sites, the H helix and the GXXLE region (through Leu(309)), appears to play a critical role in encapsulation of the substrate...
  44. ncbi Low temperature of GroEL/ES overproduction permits growth of Escherichia coli cells lacking trigger factor DnaK
    S Vorderwülbecke
    Ciphergen Biosystems GmbH, Hannah Vogt Str 1, 37085 Göttingen, Germany
    FEBS Lett 579:181-7. 2005
    ..GroEL/GroES thus influences the folding of proteins previously identified as DnaK/TF substrates...
  45. ncbi Monitoring macromolecular complexes involved in the chaperonin-assisted protein folding cycle by mass spectrometry
    Esther van Duijn
    Department of Biomolecular Mass Spectrometry, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Sorbonnelaan 16, 3584 CA Utrecht, The Netherlands
    Nat Methods 2:371-6. 2005
    ..A major advantage of native mass spectrometry is that, given sufficient resolution, it allows the analysis at the picomole level of sensitivity of heterogeneous protein complexes with molecular masses up to several million daltons...
  46. pmc Revisiting the GroEL-GroES reaction cycle via the symmetric intermediate implied by novel aspects of the GroEL(D398A) mutant
    Ayumi Koike-Takeshita
    Department of Medical Genome Sciences, Graduate School of Frontier Sciences, The University of Tokyo, Kashiwa, Chiba, Japan
    J Biol Chem 283:23774-81. 2008
    ..In light of these results, the current model of the GroEL-GroES reaction cycle via the asymmetric 1:1 GroEL-GroES complex deserves reexamination...
  47. ncbi GroEL-substrate-GroES ternary complexes are an important transient intermediate of the chaperonin cycle
    Takuya Miyazaki
    Department of Biotechnology, Faculty of Engineering, Tottori University, Tottori 680 8552, Japan
    J Biol Chem 277:50621-8. 2002
    ..The behavior of GroEL C138W was reflected closely in its in vivo characteristics, demonstrating the importance of this conformational change to the overall activity of GroEL...
  48. ncbi The ins and outs of GroEL-mediated protein folding
    J S Weissman
    Howard Hughes Medical Institute, Department of Cellular and Molecular Pharmacology, University of California-San Francisco, San Francisco, CA 94143, USA
    Mol Cell 8:730-2. 2001
    ..The second defines a confinement-independent pathway, which allows GroEL to assist folding of substrates too large to be encapsulated...
  49. pmc Coexpression of UmuD' with UmuC suppresses the UV mutagenesis deficiency of groE mutants
    C E Donnelly
    Department of Biology, Massachusetts Institute of Technology, Cambridge 02139
    J Bacteriol 174:3133-9. 1992
    ..Instead we found that the presence of UmuD' increased the stability of UmuC in groE strains. In addition, we obtained evidence which indicates that GroEL interacts directly with UmuC...
  50. ncbi Complex effects of molecular chaperones on the aggregation and refolding of fibroblast growth factor-1
    K L Edwards
    Department of Pharmaceutical Chemistry, University of Kansas, 2095 Constant Avenue, Lawrence, Kansas 66047, USA
    Arch Biochem Biophys 393:14-21. 2001
    ..FGF-1 does, therefore, interact with molecular chaperones, although this may involve both the MG and the native states of the protein...
  51. pmc Trigger factor is involved in GroEL-dependent protein degradation in Escherichia coli and promotes binding of GroEL to unfolded proteins
    O Kandror
    Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA
    EMBO J 14:6021-7. 1995
    ..Thus, TF is a rate-limiting factor for CRAG degradation; it appears to regulate GroEL function and to promote the formation of TF-GroEL-CRAG complexes which are critical for proteolysis...
  52. ncbi GroEL/GroES-mediated folding of a protein too large to be encapsulated
    T K Chaudhuri
    Howard Hughes Medical Institute, Department of Genetics, Yale University School of Medicine, Boyer Center, New Haven, CT 06510, USA
    Cell 107:235-46. 2001
    ..Following the phase of ATP/GroES-dependent refolding, GroEL stably bound apoaconitase, releasing active holoenzyme upon Fe(4)S(4) cofactor formation, independent of ATP and GroES...
  53. ncbi Excluded volume effects on the refolding and assembly of an oligomeric protein. GroEL, a case study
    A Galan
    Unidad de Biofisica (Consejo Superior de Investigaciones Cientificas-Universidad del Pais Vasco (CSIC-UPV)) y Departamento de Bioquimica y Biologia Molecular, Universidad del Pais Vasco, Aptdo. 644, 48080 Bilbao, Spain
    J Biol Chem 276:957-64. 2001
    ..Our data demonstrate that the spontaneous refolding and assembly of homo-oligomeric proteins, such as GroEL, can occur efficiently (70%) under crowding conditions similar to those expected in vivo...
  54. ncbi Chaperonin-mediated de novo generation of prion protein aggregates
    J Stockel
    Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Martinsried, D 82152, Germany
    J Mol Biol 313:861-72. 2001
    ..These results show that chaperonins of the Hsp60 class can, in principle, mediate PrP aggregation de novo, i.e. independently of a pre-existent PrP(Sc) template...
  55. ncbi Purification and characterization of the GroESLx chaperonins from the symbiotic X-bacteria in Amoeba proteus
    G H Jung
    School of Biological Sciences, Seoul, 151-742, Korea
    Protein Expr Purif 23:459-67. 2001
    ..In this study, we developed a method for the purification of GroESLx and demonstrated that their chaperonin function is homologous to GroESL of E. coli...
  56. ncbi Assembly of chaperonin complexes
    A R Kusmierczyk
    Department of Molecular Biology, Cell Biology, and Biochemistry, Brown University, Box G-J2, Providence, RI 02912, USA
    Mol Biotechnol 19:141-52. 2001
    ..Interestingly, the intracellular assembly of type I chaperonins appears to be a chaperone-dependent process itself and requires functional preformed chaperonin complexes...
  57. ncbi Folding of malate dehydrogenase inside the GroEL-GroES cavity
    J Chen
    Department of Chemistry, University of Nebraska, Lincoln, Nebraska 68588, USA
    Nat Struct Biol 8:721-8. 2001
    ..Moreover, deprotection is broadly distributed throughout MDH, suggesting that it results from breaking hydrogen bonds between MDH and the cavity wall or global destabilization, as opposed to forced mechanical unfolding...
  58. ncbi Isolation and analysis of mutant alleles of the Bacillus subtilis HrcA repressor with reduced dependency on GroE function
    Silke Reischl
    Institute of Genetics, University of Bayreuth, Universitaetsstrasse 30, Bayreuth D 95440, Germany
    J Biol Chem 277:32659-67. 2002
    ..All these experimental data are in full agreement with our previously published model that HrcA needs the GroE chaperonin system for activation...
  59. pmc Cooperation of GroEL/GroES and DnaK/DnaJ heat shock proteins in preventing protein misfolding in Escherichia coli
    A Gragerov
    Institute of Molecular Genetics, Russian Academy of Sciences, Moscow
    Proc Natl Acad Sci U S A 89:10341-4. 1992
    ..Our data suggest that the GroEL and GroES proteins and the DnaK and DnaJ proteins have complementary functions in the folding and assembly of most proteins...
  60. ncbi ClpB and HtpG facilitate de novo protein folding in stressed Escherichia coli cells
    J G Thomas
    Department of Chemical Engineering, University of Washington, Seattle 98195, USA
    Mol Microbiol 36:1360-70. 2000
    ..coli cells, presumably by expanding the ability of the DnaK-DnaJ-GrpE team to interact with newly synthesized polypeptides...
  61. pmc Molecular analysis of the Haemophilus ducreyi groE heat shock operon
    L M Parsons
    Wadsworth Center for Laboratories and Research, New York State Department of Health, Albany
    Infect Immun 60:4111-8. 1992
    ..Also, H. ducreyi groE mRNA and GroEL were expressed and inducible by heat in E. coli. This is the first report describing the cloning, sequencing, and expression of H. ducreyi protein-encoding genes...
  62. ncbi Dual function of protein confinement in chaperonin-assisted protein folding
    A Brinker
    Department of Cellular Biochemistry, Max-Planck-Institute of Biochemistry, 82152 Martinsried, Germany
    Cell 107:223-33. 2001
    ....
  63. doi A study of the antigenicity of Rickettsia helvetica proteins using two-dimensional gel electrophoresis
    Nedaa Hajem
    School of Sustainable Development of Society and Technology, Malardalens University, Eskilstuna, Sweden
    APMIS 117:253-62. 2009
    ..helvetica proteins, three other antigens exist: a 60 kDa GroEL protein, a 10 kDa GroES protein and a hitherto unknown 35 kDa hypothetical protein that has similarities with ORF-RC0799 of Rickettsia conorii...
  64. ncbi Molecular cloning of groESL locus, and purification and characterization of chaperonins, GroEL and GroES, from Bacillus brevis
    M Tokunaga
    Laboratory of Applied and Molecular Microbiology, Faculty of Agriculture, Kagoshima University, Korimoto, Japan
    Biosci Biotechnol Biochem 65:1379-87. 2001
    ..GroEL was estimated to contain 22% alpha-helix, 24% beta-sheet, and 19% turn structures, by CD measurement. GroES protein was also highly purified to examine its chaperonin activity...
  65. ncbi Characterization of heat-shock response of the marine bacterium Vibrio harveyi
    G Klein
    Department of Biochemistry, University of Gdansk, Poland
    Mol Microbiol 16:801-11. 1995
    ..V. harveyi GroES protein had a lower molecular mass (14.5 kDa) than E. coli GroES, migrating in SDS-PAGE as 15kDa protein...
  66. ncbi Structural stability of oligomeric chaperonin 10: the role of two beta-strands at the N and C termini in structural stabilization
    Isao Sakane
    Department of Biotechnology, Faculty of Engineering, Institute of Regenerative Medicine and Biofunction, Graduate School of Medical Science, Tottori University, Koyama Minami, Tottori 680 8552, Japan
    J Mol Biol 344:1123-33. 2004
    ..From analyses of the mutants' stabilities, it was revealed that the anti-parallel beta-strands at the subunit interface are crucial for subunit association and stabilization of the heptameric GroES protein.
  67. pmc ATP-triggered ADP release from the asymmetric chaperonin GroEL/GroES/ADP7 is not the rate-limiting step of the GroEL/GroES reaction cycle
    Navneet K Tyagi
    Howard Hughes Medical Institute, Department of Genetics, Yale University School of Medicine, Boyer Center, 295 Congress Avenue, New Haven, CT 06510, USA
    FEBS Lett 584:951-3. 2010
    The GroEL/GroES protein folding chamber is formed and dissociated by ATP binding and hydrolysis...
  68. ncbi Cloning and sequence of the groESL heat-shock operon of Pasteurella multocida
    B C Love
    Department of Pathology, Microbiology, and Immunology, School of Veterinary Medicine, University of California, Davis 95616, USA
    Gene 166:179-80. 1995
    ..The isolated genomic fragment was found to contain two open reading frames, the sequences of which were highly homologous to the prokaryotic groES and groEL families of genes...
  69. pmc The GroE chaperonin machine is a major modulator of the CIRCE heat shock regulon of Bacillus subtilis
    A Mogk
    Institute of Genetics, University of Bayreuth, Germany
    EMBO J 16:4579-90. 1997
    ..These results suggest that the GroE chaperonin machine modulates the activity of the HrcA repressor and therefore point to a novel function of GroE as a modulator of the heat shock response...
  70. pmc Interplay of structure and disorder in cochaperonin mobile loops
    S J Landry
    Department of Biochemistry, Tulane University School of Medicine, New Orleans, LA 70112 2699, USA
    Proc Natl Acad Sci U S A 93:11622-7. 1996
    ..Thermodynamic considerations suggest that flexible disorder in the cochaperonin mobile loops moderates their affinity for GroEL to facilitate cycles of chaperonin-mediated protein folding...
  71. ncbi A second groEL-like gene, organized in a groESL operon is present in the genome of Synechocystis sp. PCC 6803
    C Lehel
    Institute of Biochemistry, Hungarian Academy of Sciences, Szeged
    J Biol Chem 268:1799-804. 1993
    ..2-kb transcript of groESL operon increased 100-fold within 15 min upon heat stress. A 9-base pair inverted repeat revealed around the groESL promoter might be involved in regulation of the heat shock response...
  72. ncbi Co-translational binding of GroEL to nascent polypeptides is followed by post-translational encapsulation by GroES to mediate protein folding
    Bei Wen Ying
    Department of Medical Genome Sciences, Graduate School of Frontier Sciences, The University of Tokyo, FSB 401, 5 1 5 Kashiwanoha, Kashiwa, Chiba 277 8562, Japan
    J Biol Chem 281:21813-9. 2006
    ..GroEL holds the nascent chain on the ribosome in a polypeptide length-dependent manner and post-translationally encapsulates the polypeptide using the GroES cap to accomplish the chaperonin-mediated folding process...
  73. ncbi An improved strategy for high-level production of TEV protease in Escherichia coli and its purification and characterization
    Lei Fang
    The State Key Laboratory of Pharmaceutical Biotechnology and Department of Biochemistry, College of Life Science, Nanjing University, Nanjing 210093, PR China
    Protein Expr Purif 51:102-9. 2007
    ..The enzyme activity of His6-TEV was generally characterized by using GST-EGFP and His6-L-TNF fusion protein as substrates, which contained a TEV cleavage site between two moieties...
  74. pmc A chaperone network controls the heat shock response in E. coli
    Eric Guisbert
    Department of Biochemistry and Biophysics, Microbiology and Immunology, and Stomatology, University of California, San Francisco, San Francisco, California 94143, USA
    Genes Dev 18:2812-21. 2004
    ..We discuss why using a chaperone network to regulate sigma32 results in a more sensitive and accurate detection of the protein folding environment...
  75. pmc PCR amplification and comparison of nucleotide sequences from the groESL heat shock operon of Ehrlichia species
    J W Sumner
    Viral and Rickettsial Zoonoses Branch, Centers for Disease Control and Prevention, Atlanta, Georgia 30333, USA
    J Clin Microbiol 35:2087-92. 1997
    ..phagocytophila. A single pair of PCR primers derived from these sequences was used to detect E. chaffeensis and HGE agent DNA in blood samples from human patients with ehrlichiosis...
  76. ncbi The sequence of the groES and groEL genes from the mouse pneumonitis agent of Chlamydia trachomatis
    Y Ho
    Maxwell Finland Laboratory for Infectious Diseases, Boston City Hospital, Boston University School of Medicine, MA 02118
    Gene 141:143-4. 1994
    ..At the amino-acid level, the MoPn Hsp60 shows a 99% identity with those from C. trachomatis human strains. In a mouse model, MoPn Hsp60 could prove useful in deciphering the pathogenesis of human chlamydial diseases...
  77. ncbi Identification of nucleotide-binding regions in the chaperonin proteins GroEL and GroES
    J Martin
    Cellular Biochemistry and Biophysics Program, Memorial Sloan Kettering Cancer Center, New York 10021
    Nature 366:279-82. 1993
    ..ATP binding to GroES may be important in charging the seven subunits of the interacting GroEL ring with ATP to facilitate cooperative ATP binding and hydrolysis for substrate protein release...
  78. ncbi Improving the productivity of recombinant protein in Escherichia coli under thermal stress by coexpressing GroELS chaperone system
    So Yeon Kim
    Department of Chemical and Biochemical Engineering, and Institute for Environmental Technology and Industry, Pusan National University, Busan, Korea
    J Microbiol Biotechnol 19:72-7. 2009
    ..coli is not efficient. This study indicates that the employment of the GroELS overexpression system can expand the range of environmental conditions for E. coli...
  79. pmc Multi-scale simulations provide supporting evidence for the hypothesis of intramolecular protein translocation in GroEL/GroES complexes
    Ivan Coluzza
    Department of Chemistry, University of Cambridge, Cambridge, United Kingdom
    PLoS Comput Biol 4:e1000006. 2008
    ....
  80. doi Monitoring protein conformation along the pathway of chaperonin-assisted folding
    Shruti Sharma
    Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18, D 82152 Martinsried, Germany
    Cell 133:142-53. 2008
    ..Segmental chain release and compaction may be important in avoiding misfolding by proteins that fail to fold efficiently through spontaneous hydrophobic collapse...
  81. doi PCR-RFLP assay for species and subspecies differentiation of the Streptococcus bovis group based on groESL sequences
    Hsiao Jan Chen
    Department of Clinical Laboratory Sciences and Medical Biotechnology, National Taiwan University College of Medicine, Taipei, Taiwan
    J Med Microbiol 57:432-8. 2008
    ..Restriction digestion of the amplicon with AclI further differentiated the species and subspecies...
  82. ncbi Increased expression and purification of soluble iron-regulatory protein 1 from Escherichia coli co-expressing chaperonins GroES and GroEL
    H Carvalho
    Departamento de Ciencias Biologicas, Universidade Federal de Sao Paulo, Diadema, SP, Brasil
    Braz J Med Biol Res 41:270-6. 2008
    ..These results corroborate previous studies, which suggest the use of folding catalysts as a powerful strategy to increase protein solubility when expressing heterologous proteins in E. coli...
  83. ncbi Identification & differentiation of Mycobacterium avium & M. intracellulare by PCR- RFLP assay using the groES gene
    V Aravindhan
    Tuberculosis Research Centre, Chennai, India
    Indian J Med Res 126:575-9. 2007
    ..We report a new polymerase chain reaction (PCR) - restriction fragment length polymorphism (RFLP) assay using mycobacterial groES as a target to identify Mycobacterium avium and M. intracellulare in clinical samples...
  84. pmc Interaction of the heat shock protein GroEL of Escherichia coli with single-stranded DNA-binding protein: suppression of ssb-113 by groEL46
    P S Laine
    Department of Biological Sciences, University of Cincinnati, Ohio 45221
    J Bacteriol 174:3204-11. 1992
    ..The mechanism of suppression of ssb-113 by groEL46 appears to differ from that of ssb-1 by groEL411. The data suggest that GroEL may interact with single-stranded DNA-binding protein in more than one domain...
  85. ncbi The Escherichia coli groE chaperonins
    C Georgopoulos
    Department of Cellular, Viral and Molecular Biology, University of Utah Medical Center, Salt Lake City 84132
    Semin Cell Biol 1:19-25. 1990
    ..The proposed role of the groES chaperonin is to displace the polypeptides bound to groEL, thus effectively promoting the recycling of groEL...
  86. pmc A role for confined water in chaperonin function
    Jeremy L England
    James H Clark Center, S297, Stanford University, Stanford, California 94305, USA
    J Am Chem Soc 130:11838-9. 2008
    ..Our results suggest a novel view of the behavior of confined water for models of in vivo protein folding scenarios...
  87. ncbi The 69 kDa Escherichia coli maltodextrin glucosidase does not get encapsulated underneath GroES and folds through trans mechanism during GroEL/GroES-assisted folding
    Subhankar Paul
    Department of Biochemical Engineering and Biotechnology, Indian Institute of Technology Delhi, Hauz Khas, New Delhi 110016, India
    FASEB J 21:2874-85. 2007
    ..GroES could not encapsulate GroEL-bound MalZ. All these experimental findings suggested that GroEL/GroES-assisted folding of MalZ followed trans mechanism, whereas denatured MalZ and GroES bound to the opposite rings of a GroEL molecule...
  88. ncbi Global transcriptome analysis of the heat shock response of Bifidobacterium longum
    Enea Rezzonico
    Nestle Research Center, Vers chez les Blanc, Lausanne, Switzerland
    FEMS Microbiol Lett 271:136-45. 2007
    ..longum cells to heat shock was suggested by the induction of the gene encoding the tmRNA-associated small protein B (SmpB) with concomitant high constitutive expression of the tmRNA gene...
  89. pmc Folding trajectories of human dihydrofolate reductase inside the GroEL GroES chaperonin cavity and free in solution
    Reto Horst
    Department of Molecular Biology and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA 92037, USA
    Proc Natl Acad Sci U S A 104:20788-92. 2007
    ....
  90. ncbi Impaired assembly of E1 decarboxylase of the branched-chain alpha-ketoacid dehydrogenase complex in type IA maple syrup urine disease
    R M Wynn
    Departments of Biochemistry and Internal Medicine, University of Texas Southwestern Medical Center, Dallas, Texas 75235 9038, USA
    J Biol Chem 273:13110-8. 1998
    ..The mutations involving the C-terminal aromatic residues impede both the kinetics of subunit assembly and the formation of the native alpha2 beta2 structure...
  91. ncbi BeF(x) stops the chaperonin cycle of GroEL-GroES and generates a complex with double folding chambers
    Hideki Taguchi
    Chemical Resources Laboratory, Tokyo Institute of Technology, 4259 Nagatsuta, Yokohama, 226 8503, Japan
    J Biol Chem 279:45737-43. 2004
    ..Thus, BeF(x) stabilizes two GroEL-GroES complexes; one with a single folding chamber and the other with double folding chambers. These results shed light on the intermediate ADP.P(i) nucleotide states in the functional cycle of GroEL...
  92. ncbi Uniform and residue-specific 15N-labeling of proteins on a highly deuterated background
    Jocelyne Fiaux
    Institut fur Molekularbiologie und Biophysik, Eidgenossische Technische Hochschule Zurich, CH 8093 Zurich, Switzerland
    J Biomol NMR 29:289-97. 2004
    ....
  93. ncbi Genetic immunization with Ehrlichia ruminantium GroEL and GroES homologues
    Alri Pretorius
    Molecular Biology Section, Onderstepoort Veterinary Institute, Pretoria, South Africa
    Ann N Y Acad Sci 969:151-4. 2002
    ..None of the mice inoculated with the genetic vaccine survived. Immunological memory was also tested in these mice and a correlation between splenocyte proliferation and the survival rate was observed...
  94. ncbi Crystal structures of the group II chaperonin from Thermococcus strain KS-1: steric hindrance by the substituted amino acid, and inter-subunit rearrangement between two crystal forms
    Yasuhito Shomura
    Department of Chemistry, Graduate School of Science, Kyoto University, Sakyo ku, Kyoto 606 8502, Japan
    J Mol Biol 335:1265-78. 2004
    ..The crystal structure obtained at the lower concentration of sulfate ion tilts outward, and has much looser inter-subunit contacts compared with those in the presence of a higher concentration of sulfate ion...
  95. ncbi Archaeal group II chaperonin mediates protein folding in the cis-cavity without a detachable GroES-like co-chaperonin
    Takao Yoshida
    Kamaishi Laboratories, Marine Biotechnology Institute Co Ltd, 3 75 1 Heita, Kamaishi, 026 0001, Iwate, Japan
    J Mol Biol 315:73-85. 2002
    ..The present data indicate that, in the group II chaperonin of Thermococcus strain KS-1, the protein folding proceeds in its cis-ring in an ATP-dependent fashion without any co-chaperonin...
  96. ncbi Gene structure and transcriptional regulation specific to the groESL operon from the psychrophilic bacterium Colwellia maris
    Seiji Yamauchi
    Graduate School of Science and Engineering, Ehime University, 790 8577, Matsuyama, Ehime, Japan
    Arch Microbiol 180:272-8. 2003
    ..coli. The low G+C content may be important for maintaining transcription at low temperatures...
  97. ncbi Cloning and characterization of the groE heat-shock operon of the marine bacterium Vibrio harveyi
    Dorota Kuchanny-Ardigò
    Department of Biochemistry, University of Gdansk, Kładki 24, 80 822 Gdansk, Poland
    Microbiology 149:1483-92. 2003
    ..The results suggest that the GroEL chaperone may be more species-specific than the GroES co-chaperone...
  98. ncbi Dissociation of the GroEL-GroES asymmetric complex is accelerated by increased cooperativity in ATP binding to the GroEL ring distal to GroES
    Yael Fridmann
    Department of Structural Biology, Weizmann Institute of Science, Rehovot 76100, Israel
    Biochemistry 41:5938-44. 2002
    ..It is shown that the rate of complex dissociation increases with increasing positive cooperativity in ATP binding by the GroEL ring distal to GroES in the GroEL-GroES complex...
  99. ncbi Serological association between Chlamydia pneumoniae infection and age-related macular degeneration
    Murat V Kalayoglu
    Department of Ophthalmology, Massachusetts Eye and Ear Infirmary, Ophthalmic Education Center, Boston 02114, USA
    Arch Ophthalmol 121:478-82. 2003
    ..It is therefore plausible that this microorganism also contributes to the pathogenesis of ARMD...
  100. pmc Atomic-level observation of macromolecular crowding effects: escape of a protein from the GroEL cage
    Adrian H Elcock
    Department of Biochemistry, University of Iowa, Iowa City, IA 52242, USA
    Proc Natl Acad Sci U S A 100:2340-4. 2003
    ....
  101. ncbi Mice immune responses to Brucella abortus heat shock proteins. Use of baculovirus recombinant-expressing whole insect cells, purified Brucella abortus recombinant proteins, and a vaccinia virus recombinant as immunogens
    J E Bae
    Department of Biomedical Sciences and Pathobiology, Center for Molecular Medicine and Infectious Diseases, Virginia Maryland Regional College of Veterinary Medicine, Virginia Polytechnic Institute and State University, 24061 0342, Blacksburg, VA, USA
    Vet Microbiol 88:189-202. 2002
    ..Based on the results obtained, we suggest that although humoral and cell-mediated immune responses are induced, but protective immune response is not induced by B. abortus HSPs...

Research Grants46

  1. Chaperonin-mediated protein folding
    Arthur Horwich; Fiscal Year: 2007
    ....
  2. TARGETING OF HUMAN OTC TO THE MITOCHONDRIAL MATRIX
    Arthur Horwich; Fiscal Year: 1992
    ..In vitro synthesized precursors with either reactive amino acid side chains or enzymatically active mature portions will also be used as affinity- labeling reagents, to identify additional interacting mitochondrial components...
  3. GROEL-MEDIATED PROTEIN FOLDING
    Arthur Horwich; Fiscal Year: 2000
    ..I.'s laboratory, in conjunction with GroEL-mutant "traps" that are capable of binding but not releasing non-native polypeptides, will be used to test these hypotheses. ..
  4. MECHANISM OF ACTION OF THE HSP100 CHAPERONE CLPA
    Arthur Horwich; Fiscal Year: 2006
    ....
  5. FUNCTION OF GROEL IN THE BACTERIAL CYTOPLASM
    Arthur Horwich; Fiscal Year: 1993
    ....
  6. Structural Dynamics of Biomolecular Systems
    Ivet Bahar; Fiscal Year: 2009
    ..These aims will be pursued in collaboration with the National Center for Biomedical Computing Simbios at Stanford U. ..
  7. Bridging Sequence Patterns and Structural Dynamics
    Ivet Bahar; Fiscal Year: 2009
    ....
  8. Computational and experimental studies of targets of protein kinase inhibitors
    ADRIAN HAMILTON ELCOCK; Fiscal Year: 2010
    ..The research proposed here directly addresses the single greatest challenge to the therapeutic pursuit of kinases: how to design small molecule inhibitors that can specifically inhibit a kinase of interest. ..
  9. Bridging Sequence Patterns and Structural Dynamics
    Ivet Bahar; Fiscal Year: 2010
    ....
  10. Structural Dynamics of Biomolecular Systems
    Ivet Bahar; Fiscal Year: 2010
    ..abstract_text> ..
  11. Computational Prediction of Biomolecular Dynamics
    Ivet Bahar; Fiscal Year: 2007
    ..This novel computational methodology will fill a unique niche due to its applicability to large structures and assemblies, its speed and accessibility to the scientific community. ..
  12. Multiscale Dynamics of Cell Cycle Control and Apoptosis
    Ivet Bahar; Fiscal Year: 2005
    ....
  13. Computational and experimental studies of targets of protein kinase inhibitors
    ADRIAN ELCOCK; Fiscal Year: 2007
    ..The research proposed here directly addresses the single greatest challenge to the therapeutic pursuit of kinases: how to design small molecule inhibitors that can specifically inhibit a kinase of interest. ..
  14. Alignment-independent Classification of Proteins
    Ivet Bahar; Fiscal Year: 2007
    ....
  15. Systems analysis of oxygen regulation in Halobacterium
    AMY SCHMID; Fiscal Year: 2007
    ..These proposed experiments are expected to result in a transcriptional network model that addresses how organisms maintain homeostasis despite stress. ..
  16. Molecular Simulations of Folding & Association in Physiological Environments
    ADRIAN HAMILTON ELCOCK; Fiscal Year: 2010
    ..biological and quantitative proteomics data will be utilized to build preliminary 3D models of four different environments in the model prokaryote Escherichia coli: the cytoplasm, periplasm, and inner and outer-membranes ..