protein renaturation

Summary

Summary: The reconstitution of a protein's activity following denaturation.

Top Publications

  1. Mayor U, Guydosh N, Johnson C, Grossmann J, Sato S, Jas G, et al. The complete folding pathway of a protein from nanoseconds to microseconds. Nature. 2003;421:863-7 pubmed
    ..Molecular dynamics simulations give rate constants and structural details highly consistent with experiment, thereby completing the description of folding at atomic resolution. ..
  2. Ho J, Middelberg A, Ramage P, Kocher H. The likelihood of aggregation during protein renaturation can be assessed using the second virial coefficient. Protein Sci. 2003;12:708-16 pubmed
    ..SVC measurements provide a useful link, for protein folding and aggregation, between empirical observation and thermodynamics. ..
  3. Jemth P, Day R, Gianni S, Khan F, Allen M, Daggett V, et al. The structure of the major transition state for folding of an FF domain from experiment and simulation. J Mol Biol. 2005;350:363-78 pubmed
    ..There are some differences in the details and interpretation of specific Phi-values. ..
  4. Capaldi A, Kleanthous C, Radford S. Im7 folding mechanism: misfolding on a path to the native state. Nat Struct Biol. 2002;9:209-16 pubmed
    ..The data also demonstrate that non-native interactions can play a significant role in folding, even for small proteins with simple topologies. ..
  5. Nath D, Rao M. Artificial chaperone mediated refolding of xylanase from an alkalophilic thermophilic Bacillus sp. Implications for in vitro protein renaturation via a folding intermediate. Eur J Biochem. 2001;268:5471-8 pubmed
    ..The relevance of our findings to the role of artificial chaperones in vivo is discussed. ..
  6. Park S. Hydrophobic core variant ubiquitin forms a molten globule conformation at acidic pH. J Biochem Mol Biol. 2004;37:676-83 pubmed
    ..This observation suggests that the equilibrium molten globule state of hydrophobic core variant ubiquitin is an on-pathway folding intermediate. ..
  7. Nuc P, Nuc K. [Recombinant protein production in Escherichia coli]. Postepy Biochem. 2006;52:448-56 pubmed
    ..With its wealth of available mutants tested is the best suited to economically test new gene constructs and to scale up the recombinant protein production. ..
  8. Cherish Babu P, Srinivas V, Krishna Mohan V, Krishna E. Renaturation, purification and characterization of streptokinase expressed as inclusion body in recombinant E. coli. J Chromatogr B Analyt Technol Biomed Life Sci. 2008;861:218-26 pubmed
    ..Size exclusion chromatography profile shows that there are minimal aggregates in the active streptokinase protein and the percentage of renaturation is around 99%. ..
  9. Xiao Yan Z, Su Xia L, Qin Sheng Y. The renaturation of procarboxypeptidase B by urea gradient gel filtration and some properties of recombinant carboxypeptidase B. Protein Pept Lett. 2005;12:671-6 pubmed
    ..The two-dimension electrophoresis map of rCPB showed that the pI value of rCPB was 5.35. UV absorbance spectrum of the enzyme showed that an absorbance maximum was at 277 nm. ..

More Information

Publications62

  1. Zietkiewicz S, Lewandowska A, Stocki P, Liberek K. Hsp70 chaperone machine remodels protein aggregates at the initial step of Hsp70-Hsp100-dependent disaggregation. J Biol Chem. 2006;281:7022-9 pubmed
    ..The binding of extracted GFP molecules to the GroEL trap prevented their reaggregation. We propose that the Hsp70 machine disentangles polypeptides from protein aggregates prior to Hsp100 action. ..
  2. Rumfeldt J, Stathopulos P, Chakrabarrty A, Lepock J, Meiering E. Mechanism and thermodynamics of guanidinium chloride-induced denaturation of ALS-associated mutant Cu,Zn superoxide dismutases. J Mol Biol. 2006;355:106-23 pubmed
  3. Jemth P, Johnson C, Gianni S, Fersht A. Demonstration by burst-phase analysis of a robust folding intermediate in the FF domain. Protein Eng Des Sel. 2008;21:207-14 pubmed publisher
    ..The intermediate appears robust to changing conditions and thus fulfils an important criterion for a productive molecular species on the folding reaction pathway. ..
  4. Thorpe I, Zhou J, Voth G. Peptide folding using multiscale coarse-grained models. J Phys Chem B. 2008;112:13079-90 pubmed publisher
    ..These findings suggest that MS-CG models may be of significant utility in the study of peptide folding. ..
  5. Kobashigawa Y, Nishimiya Y, Miura K, Ohgiya S, Miura A, Tsuda S. A part of ice nucleation protein exhibits the ice-binding ability. FEBS Lett. 2005;579:1493-7 pubmed
    ..These data imply that a part of INP constructs a unique structure so as to interact with the ice crystal surfaces. ..
  6. Zeeb M, Balbach J. Millisecond protein folding studied by NMR spectroscopy. Protein Pept Lett. 2005;12:139-46 pubmed
    ..Together with an overview of current achievements within this field, we present millisecond protein folding studies by NMR of the cold shock protein CspB from Bacillus subtilis. ..
  7. Pappenberger G, Bachmann A, Müller R, Aygün H, Engels J, Kiefhaber T. Kinetic mechanism and catalysis of a native-state prolyl isomerization reaction. J Mol Biol. 2003;326:235-46 pubmed
  8. Nair V, Kamboj R. Inhibition of inosine monophosphate dehydrogenase (IMPDH) by 2-[2-(Z)-fluorovinyl]inosine 5'-monophosphate. Bioorg Med Chem Lett. 2003;13:645-7 pubmed
    ..Inhibition of IMPDH appears to be irreversible with k(inact) and K(i) values of 0.0269 s(-1) and 1.11 microM, respectively. ..
  9. Bronsoms S, Villanueva J, Canals F, Querol E, Aviles F. Analysis of the effect of potato carboxypeptidase inhibitor pro-sequence on the folding of the mature protein. Eur J Biochem. 2003;270:3641-50 pubmed
    ..coli. However, structural analysis by spectroscopy, hydrogen exchange and limited proteolysis by mass spectrometry, indicate the capability of such N-terminal pro-sequence to fold within the precursor form. ..
  10. Ruiz J, Ferrer J, Pire C, Llorca F, Bonete M. Denaturation studies by fluorescence and quenching of thermophilic protein NAD+-glutamate dehydrogenase from Thermus thermophilus HB8. J Protein Chem. 2003;22:295-301 pubmed
    ..Fluorescence quenching by external quenchers, KI and acrylamide, has also been carried out. ..
  11. Yang X, Dong X, Li Y, Wang Y, Chen W. Purification and refolding of a novel cancer/testis antigen BJ-HCC-2 expressed in the inclusion bodies of Escherichia coli. Protein Expr Purif. 2004;33:332-8 pubmed
    ..This method of protein purification and refolding is easy to manipulate and may be applicable to the hydrophobic proteins that are unable to be purified by other methods. ..
  12. Hirai M, Koizumi M, Hayakawa T, Takahashi H, Abe S, Hirai H, et al. Hierarchical map of protein unfolding and refolding at thermal equilibrium revealed by wide-angle X-ray scattering. Biochemistry. 2004;43:9036-49 pubmed
    ..This map can visualize a detailed feature of the unfolding-refolding transition of a protein depending on various structural hierarchical levels; however, the exact meaning of the map will await sharpening by additional works. ..
  13. Ballet T, Brukert F, Mangiagalli P, Bureau C, Boulangé L, Nault L, et al. DnaK prevents human insulin amyloid fiber formation on hydrophobic surfaces. Biochemistry. 2012;51:2172-80 pubmed publisher
    ..As this peptide is also a known DnaK substrate, our data indicate that the peptide and the chaperone might compete for a common site during the process of insulin aggregation on hydrophobic surfaces. ..
  14. Deng X, Zheng Y, Yu F, Ning B, Jiang Y. [Preparation and the anti-tumor activity of mutant Staphylococcal enterotoxin B]. Xi Bao Yu Fen Zi Mian Yi Xue Za Zhi. 2004;20:360-2 pubmed
    ..The anti-tumor activity of the mutant SEB-K172E is much higher than that of wild-type SEB, suggesting that the mutant SEB-K172E may become a potential anti-tumor drug. ..
  15. Gasanov E, Demidyuk I, Shubin A, Kozlovskiy V, Leonova O, Kostrov S. Hetero- and auto-activation of recombinant glutamyl endopeptidase from Bacillus intermedius. Protein Eng Des Sel. 2008;21:653-8 pubmed publisher
    ..This approach makes it possible to produce the enzyme without extrinsic proteinases, which is a prerequisite for using it in limited hydrolysis of proteins and peptides. ..
  16. Kundu M, Sen P, Das K. Structure, stability, and chaperone function of alphaA-crystallin: role of N-terminal region. Biopolymers. 2007;86:177-92 pubmed
    ..Detailed analysis showed that the most important role of N-terminal region is to control the oligomerization, which is crucial for the stability and in vivo survival of this protein molecule. ..
  17. Shamji M, Chen J, Friedman A, Richardson W, Chilkoti A, Setton L. Synthesis and characterization of a thermally-responsive tumor necrosis factor antagonist. J Control Release. 2008;129:179-86 pubmed publisher
    ..Potential advantages of this ELP-sTNFRII fusion protein as an anti-TNFa drug depot include facility of injection, in situ depot formation, low endotoxin content, and functionality against TNFalpha. ..
  18. Asano R, Sone Y, Ikoma K, Hayashi H, Nakanishi T, Umetsu M, et al. Preferential heterodimerization of a bispecific diabody based on a humanized anti-EGFR antibody 528. Protein Eng Des Sel. 2008;21:597-603 pubmed publisher
    ..We suggest that the preparation of hEx3 from bacterial insoluble material by means of in vitro refolding would be useful for industrial-scale production of the diabody for its potential use in clinical studies. ..
  19. Rajanikant C, Melzer M, Rao B, Sainis J. Homologous recombination properties of OsRad51, a recombinase from rice. Plant Mol Biol. 2008;68:479-91 pubmed publisher
    ..Renaturation activity was ATP dependent; however strand exchange activity was ATP independent. This is the first report on in vitro characterization of Rad51 protein from crop plants. ..
  20. Kim R, Guo J. Systematic analysis of short internal indels and their impact on protein folding. BMC Struct Biol. 2010;10:24 pubmed publisher
  21. Hou J, Sun J, Xu Z, Fan W, Zhang Y, Liu Y, et al. [Expression, purification and renaturation of Pol P51 antigen of HIV-1 strain CN54 and its application in antibody detection]. Sheng Wu Gong Cheng Xue Bao. 2010;26:201-6 pubmed
    ..The results suggested that recombinant HIV-1 P51 can be prepared as diagnostic reagent, and provides valuable support for HIV-1 detection and vaccine research. ..
  22. Tzul F, Kurchan E, Roder H, Bowler B. Competition between reversible aggregation and loop formation in denatured iso-1-cytochrome c. Biochemistry. 2009;48:481-91 pubmed publisher
  23. Kim M, Abdi K, Lee G, Rabbi M, Lee W, Yang M, et al. Fast and forceful refolding of stretched alpha-helical solenoid proteins. Biophys J. 2010;98:3086-92 pubmed publisher
    ..Our physical view of the protein component of cells as being comprised of predominantly inextensible structural elements under tension may need revision to incorporate springs. ..
  24. Saeed I, Ashraf S. Denaturation studies reveal significant differences between GFP and blue fluorescent protein. Int J Biol Macromol. 2009;45:236-41 pubmed publisher
    ..Taken together, our preliminary results show that despite being very similar in both amino acid sequences and overall structures, there may be subtle and important structural/conformational differences between BFP and GFP. ..
  25. Wu Q, Li F, Wang X. Val65 plays an important role in the substrate synergism, structural stability and activity of arginine kinase. Int J Biol Macromol. 2009;45:393-8 pubmed publisher
    ..These results provided herein suggest that amino acid residue V65 played a relatively important role in AK substrate synergism, structural stability and activity. ..
  26. Lilie H, Richter S, Bergelt S, Frost S, Gehle F. Polyionic and cysteine-containing fusion peptides as versatile protein tags. Biol Chem. 2013;394:995-1004 pubmed publisher
    ..In this context we used cysteine-containing polyionic fusion peptides for the design of immunotoxins. In general, polyionic fusion tags can be considered as a multifunctional module in protein technology. ..
  27. Li X, Zheng W, Zhang L, Yu P, Lin Y, Su L, et al. Effective electrochemical method for investigation of hemoglobin unfolding based on the redox property of heme groups at glassy carbon electrodes. Anal Chem. 2009;81:8557-63 pubmed publisher
  28. Frank A, Ramsook C, Otoo H, Tan C, Soybelman G, Rauceo J, et al. Structure and function of glycosylated tandem repeats from Candida albicans Als adhesins. Eukaryot Cell. 2010;9:405-14 pubmed publisher
    ..Together, the modeling techniques and the supporting data lead to an approach that relates structure and function in many kinds of repeat domains in fungal adhesins. ..
  29. Nekrasova O, Wulfson A, Tikhonov R, Yakimov S, Simonova T, Tagvey A, et al. A new hybrid protein for production of recombinant bacteriorhodopsin in Escherichia coli. J Biotechnol. 2010;147:145-50 pubmed publisher
    ..coli. Functional activity of recombinant bacteriorhodopsin was confirmed by spectroscopic and electrochemical assays. ..
  30. Flaugh S, Kosinski Collins M, King J. Contributions of hydrophobic domain interface interactions to the folding and stability of human gammaD-crystallin. Protein Sci. 2005;14:569-81 pubmed
    ..Specificity of domain interface interactions is likely important for preventing incorrect associations in the high protein concentrations of the lens nucleus. ..
  31. Nieuwenhuizen W, van Leeuwen S, Jack R, Egmond M, Götz F. Molecular cloning and characterization of the alkaline ceramidase from Pseudomonas aeruginosa PA01. Protein Expr Purif. 2003;30:94-104 pubmed
    ..5. The recombinant enzyme was partially characterized. This is the first report of a high yield CDase production system allowing detailed characterization of the enzyme at the molecular level. ..
  32. Lukash T, Turkivska H, Negrutskii B, El skaya A. Chaperone-like activity of mammalian elongation factor eEF1A: renaturation of aminoacyl-tRNA synthetases. Int J Biochem Cell Biol. 2004;36:1341-7 pubmed
    ..Thus, we conclude that the chaperone-like activity of eEF1A might be important for maintaining the enzymes activity in the protein synthesis compartments of mammalian cells. ..
  33. Gross M. Emergency services: a bird's eye perspective on the many different functions of stress proteins. Curr Protein Pept Sci. 2004;5:213-23 pubmed
  34. Wladyka B, Puzia K, Dubin A. Efficient co-expression of a recombinant staphopain A and its inhibitor staphostatin A in Escherichia coli. Biochem J. 2005;385:181-7 pubmed
    ..Our optimized refolding parameters allow restoration of the native conformation of the enzyme, with yields over 10-fold higher when compared with isolation from natural sources. ..
  35. Gur E, Biran D, Shechter N, Genevaux P, Georgopoulos C, Ron E. The Escherichia coli DjlA and CbpA proteins can substitute for DnaJ in DnaK-mediated protein disaggregation. J Bacteriol. 2004;186:7236-42 pubmed
    ..Here we show that in a dnaJ mutant both CbpA and DjlA are required for efficient protein dissaggregation at 42 degrees C. ..
  36. Chi C, Gianni S, Calosci N, Travaglini Allocatelli C, Engström K, Jemth P. A conserved folding mechanism for PDZ domains. FEBS Lett. 2007;581:1109-13 pubmed
    ..Moreover, the positions of the two transition states along the reaction coordinate (as given by their beta(T)-values) are fairly constant for the five PDZ domains. ..
  37. Bhattacharjee C, Saha S, Biswas A, Kundu M, Ghosh L, Das K. Structural changes of beta-lactoglobulin during thermal unfolding and refolding--an FT-IR and circular dichroism study. Protein J. 2005;24:27-35 pubmed
    ..The combined CD and FT-IR data indicated that refolded form of beta-lactoglobulin could be characterized as a molten globule state as it had native-like secondary structure and compromised tertiary structure. ..
  38. Thammavongsa V, Mancino L, Raghavan M. Polypeptide substrate recognition by calnexin requires specific conformations of the calnexin protein. J Biol Chem. 2005;280:33497-505 pubmed
  39. Brignole E, Gibson W. Enzymatic activities of human cytomegalovirus maturational protease assemblin and its precursor (pPR, pUL80a) are comparable: [corrected] maximal activity of pPR requires self-interaction through its scaffolding domain. J Virol. 2007;81:4091-103 pubmed
    ..We conclude that although the enzymatic activities of assemblin and its precursor are comparable, there may be differences in how their catalytic sites become fully activated. ..
  40. Takahashi N, Onda M, Hayashi K, Yamasaki M, Mita T, Hirose M. Thermostability of refolded ovalbumin and S-ovalbumin. Biosci Biotechnol Biochem. 2005;69:922-31 pubmed
    ..The rate of refolding of S-ovalbumin was greater than that of ovalbumin, indicating the participation, at least in part, of an increased folding rate for thermodynamic stabilization. ..
  41. Kim B, Mangala S, Hayashi K. Co-refolding of two peptide fragments derived from Agrobacterium tumefaciens beta-glucosidase with catalytic activity. FEBS Lett. 2005;579:3075-80 pubmed
  42. Chen L. Monitoring conformational changes of immobilized RNase A and lysozyme in reductive unfolding by surface plasmon resonance. Anal Chim Acta. 2009;631:96-101 pubmed publisher
    ..5 and 2.15 kcal mole(-1), respectively. The disagreement in free energy is partially accounted for by the differences of intra-molecular interactions and immobilization. ..
  43. Papageorgiou S, Solaini G. Guanidine-induced dissociation of mitochondrial F1-ATPase. Ital J Biochem. 2004;53:148-56 pubmed
    ..Our results suggest that the delta and epsilon subunits are loosely bound to alpha3beta3gamma , and play an important role in determining structural stability to isolated mitochondrial F1-ATPase. ..
  44. Khodarahmi R, Yazdanparast R. Fluorimetric study of the artificial chaperone-assisted renaturation of carbonic anhydrase: a kinetic analysis. Int J Biol Macromol. 2005;36:191-7 pubmed
    ..Based on these findings, appropriate refolding conditions could be designed to kinetically diminish the rate of off-pathway aggregation. ..
  45. Trachuk L, Letarov A, Kudelina I, Yusupova M, Chestukhina G. In vitro refolding of carboxypeptidase T precursor from Thermoactinomyces vulgaris obtained in Escherichia coli as cytoplasmic inclusion bodies. Protein Expr Purif. 2005;40:51-9 pubmed
  46. Dong X, Huang Y, Sun Y. Refolding kinetics of denatured-reduced lysozyme in the presence of folding aids. J Biotechnol. 2004;114:135-42 pubmed
    ..Moreover, their effect on improving protein refolding was additive to those of the first group. So the cooperative application of the two kinds of folding aids could result in favorable refolding rate and yield of protein. ..
  47. Singh R, Flowers R. Efficient protein renaturation using tunable hemifluorinated anionic surfactants as additives. Chem Commun (Camb). 2010;46:276-8 pubmed publisher
  48. Altschuler G, Klug D, Willison K. Unfolding energetics of G-alpha-actin: a discrete intermediate can be re-folded to the native state by CCT. J Mol Biol. 2005;353:385-96 pubmed
    ..The high value of the activation energy between native actin and a non-native folding intermediate (I(3)) is characteristic of a partially folded, molten globule state expected to contain partial secondary structure. ..
  49. Sun Z, Xia Z, Bi F, Liu J. Expression and purification of human urodilatin by small ubiquitin-related modifier fusion in Escherichia coli. Appl Microbiol Biotechnol. 2008;78:495-502 pubmed publisher
    ..77+/-0.53 microg/ml, which was similar to that of the synthetic urodilatin standard. The expression strategy presented in this study allows convenient high yield and easy purification of small recombinant peptides with native sequences. ..
  50. Fan J, Wang G, Li W, Wu Y, Liu Y. [Expression of human Fab antibody against keratin in E.coli and its renaturation]. Xi Bao Yu Fen Zi Mian Yi Xue Za Zhi. 2004;20:441-3 pubmed
    ..ELISA and Western blot showed that the renatured Fab could bind with human keratin. The successfully prepared anti-keratin Fab with binding activity to human keratin laid a solid foundation for its further application. ..
  51. Ladokhin A, Legmann R, Collier R, White S. Reversible refolding of the diphtheria toxin T-domain on lipid membranes. Biochemistry. 2004;43:7451-8 pubmed
    ..This analysis suggests that interactions at the membrane interface dominate pH-triggered insertion of DTT, implying that the folding pathway involves interfacial intermediates. ..
  52. Dechavanne V, Barrillat N, Borlat F, Hermant A, Magnenat L, Paquet M, et al. A high-throughput protein refolding screen in 96-well format combined with design of experiments to optimize the refolding conditions. Protein Expr Purif. 2011;75:192-203 pubmed publisher
    ..Thus, the method described herein is a useful tool to determine the feasibility of refolding and to identify high-yield scalable refolding conditions optimized for each individual protein. ..
  53. Wan L, Zeng L, Chen L, Huang Q, Li S, Lu Y, et al. Expression, purification, and refolding of a novel immunotoxin containing humanized single-chain fragment variable antibody against CTLA4 and the N-terminal fragment of human perforin. Protein Expr Purif. 2006;48:307-13 pubmed
    ..IC(50) of hS83P34 for leukemic cells Raji and 6T-CEM are about 0.85 and 1.3 microM individually. Whereas, CTLA4-negative endothelial cell ECV-304 is resistant to hS83P34. ..