Intrinsically unstructured proteins: re-assessing the protein structure-function paradigmP E Wright
Department of Molecular Biology and Skaggs Institute of Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA
J Mol Biol 293:321-31. 1999
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- Local structural plasticity of the prion protein. Analysis of NMR relaxation dynamics
J H Viles
Department of Molecular Biology and Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California 92037, USA
Biochemistry 40:2743-53. 2001
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- NMR structural and dynamic characterization of the acid-unfolded state of apomyoglobin provides insights into the early events in protein folding
J Yao
Department of Molecular Biology MB2, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, USA
Biochemistry 40:3561-71. 2001
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- Conformational and dynamic characterization of the molten globule state of an apomyoglobin mutant with an altered folding pathway
S Cavagnero
Department of Molecular Biology MB-2 and Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California 92037, USA
Biochemistry 40:14459-67. 2001
..These studies provide important insights into the interplay between secondary and tertiary structure formation in protein folding...
- Folding of peptide fragments comprising the complete sequence of proteins. Models for initiation of protein folding. I. Myohemerythrin
H J Dyson
Department of Molecular Biology, Scripps Research Institute, La Jolla, CA 92037
J Mol Biol 226:795-817. 1992
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- Structural and dynamic characterization of an unfolded state of poplar apo-plastocyanin formed under nondenaturing conditions
Y Bai
Department of Molecular Biology and Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California 92037, USA
Protein Sci 10:1056-66. 2001
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- Solution structure of the third immunoglobulin domain of the neural cell adhesion molecule N-CAM: can solution studies define the mechanism of homophilic binding?
A R Atkins
Department of Molecular Biology, The Scripps Research Institute, La Jolla, CA 92037, USA
J Mol Biol 311:161-72. 2001
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- Folding of immunogenic peptide fragments of proteins in water solution. II. The nascent helix
H J Dyson
Department of Molecular Biology, Research Institute of Scripps Clinic, La Jolla, CA 92037
J Mol Biol 201:201-17. 1988
..The possible role of nascent secondary structure in induction of antipeptide antibodies and in initiation of protein folding is discussed...
- Backbone dynamics in dihydrofolate reductase complexes: role of loop flexibility in the catalytic mechanism
M J Osborne
Department of Molecular Biology and Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, USA
Biochemistry 40:9846-59. 2001
..Finally, the relaxation data provide evidence for long-range motional coupling between the adenosine binding loop and distant regions of the protein...
- Sequence-dependent correction of random coil NMR chemical shifts
S Schwarzinger
Department of Molecular Biology, The Scripps Research Institute, La Jolla, California 92037, USA
J Am Chem Soc 123:2970-8. 2001
..This new set of correction factors will have important applications to folded proteins as well as to short, unstructured peptides and unfolded proteins...
- Solution structure of Escherichia coli glutaredoxin-2 shows similarity to mammalian glutathione-S-transferases
B Xia
Department of Molecular Biology and Skaggs Institute of Chemical Biology, The Scripps Research Institute, La Jolla, CA 92037, USA
J Mol Biol 310:907-18. 2001
..The primary function of Grx2 as a GST-like glutaredoxin is to catalyze reversible glutathionylation of proteins with GSH in cellular redox regulation including stress responses...
- Contribution of increased length and intact capping sequences to the conformational preference for helix in a 31-residue peptide from the C terminus of myohemerythrin
M T Reymond
Department of Molecular Biology, The Scripps Research Institute, La Jolla, California 92037, USA
Biochemistry 36:5234-44. 1997
..A compendium of results from this and previous peptide studies has also led to a novel observation, the existence of a correlation between the amide proton chemical shift and temperature coefficient...
- SANE (Structure Assisted NOE Evaluation): an automated model-based approach for NOE assignment
B M Duggan
Department of Molecular Biology MB2 and Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA 92037, USA
J Biomol NMR 19:321-9. 2001
..Use of this semi-automated iterative approach assists in the identification of errors in the NOE assignments to short-cut the path to an NMR solution structure...
- Anisotropic rotational diffusion in model-free analysis for a ternary DHFR complex
M J Osborne
Department of Molecular Biology and Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA 92037, USA
J Biomol NMR 19:209-30. 2001
..These errors can hinder our understanding of the role of internal motions in protein function...
- Potential bias in NMR relaxation data introduced by peak intensity analysis and curve fitting methods
J H Viles
Department of Molecular Biology and Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA 90237, USA
J Biomol NMR 21:1-9. 2001
..In general, a 2-parameter fit of relaxation decay curves is preferable. However, for very low intensity peaks a 3 parameter fit may be more appropriate...
- The conformational restriction of synthetic vaccines for malaria
A C Satterthwait
Research Institute of Scripps Clinic, La Jolla, CA 92037
Bull World Health Organ 68:17-25. 1990
..Polyclonal antibodies to this shaped peptide show a strong cross-reaction with living sporozoites...
- Two different neurodegenerative diseases caused by proteins with similar structures
H Mo
Department of Molecular Biology and Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA
Proc Natl Acad Sci U S A 98:2352-7. 2001
..Although the two proteins most likely arose through duplication of a single ancestral gene, the relationship is now so distant that only the structures retain similarity; the functions have diversified along with the sequence...
- Zinc finger proteins: new insights into structural and functional diversity
J H Laity
Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA
Curr Opin Struct Biol 11:39-46. 2001
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- Structure of the PHD zinc finger from human Williams-Beuren syndrome transcription factor
J Pascual
Department of Molecular Biology and Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Rd, La Jolla, CA 92037, USA
J Mol Biol 304:723-9. 2000
..The structure reveals a conserved zinc-binding core, together with two variable loops that are likely candidates for interactions between the various PHD domains and their specific ligands...
- 1H resonance assignments and secondary structure of the carbon monoxide complex of soybean leghemoglobin determined by homonuclear two-dimensional and three-dimensional NMR spectroscopy
D Morikis
Department of Molecular Biology, Scripps Research Institute, La Jolla, CA 92037
Eur J Biochem 219:611-26. 1994
..Population of a second protein conformation, in which there is perturbation at the A-G-H helix interface, is observed at low pH...
- Probing protein structure using biochemical and biophysical methods. Proteolysis, matrix-assisted laser desorption/ionization mass spectrometry, high-performance liquid chromatography and size-exclusion chromatography of p21Waf1/Cip1/Sdi1
R W Kriwacki
Department of Molecular Biology, Scripps Research Institute, La Jolla, CA 92037, USA
J Chromatogr A 777:23-30. 1997
..Our method allows a proteolytic map to be obtained from a single mass spectrum for fragments produced from a single proteolytic reaction...
