Mechanisms of protein folding

Current Opinion in Structural Biology

Volumn 11, Issue 1, 2001, Pages 70-82

  Grantcharova, Viara ^a   Alm, Eric J ^b   Baker, David ^b   Horwich, Arthur L ^c  

^a HARVARD UNIVERSITY   (United States)

^b UNIVERSITY OF WASHINGTON SCHOOL OF MEDICINE   (United States)

^c HOWARD HUGHES MEDICAL INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACYLPHOSPHATASE; ADENOSINE TRIPHOSPHATE; CHAPERONIN; CHAPERONIN GROEL; CHAPERONIN GROES; PROCARBOXYPEPTIDASE; PROTEIN; PROTEIN G; PROTEIN L; PROTEIN S6; PROTEIN SH3; PROTEIN SSO7D; PROTEIN U1A; REPRESSOR PROTEIN; TRANSCRIPTION FACTOR GCN4; UNCLASSIFIED DRUG;

ESCHERICHIA COLI; HYDROGEN BOND; HYDROLYSIS; MOLECULAR RECOGNITION; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN LOCALIZATION; PROTEIN STRUCTURE; REVIEW; TEMPERATURE;

ESCHERICHIA COLI; NEGIBACTERIA;

EID: 0035252683     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(00)00176-7     Document Type: Review

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11. Characterizing transition states in protein folding: An essential step in the puzzle
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13. Preformed secondary structure drives the association reaction of GCN4-p1, a model coiled-coil system
14. The energy landscape of a fast-folding protein mapped by Ala→Gly substitutions
15. Contribution of a buried hydrogen bond to lambda repressor folding kinetics
16. A breakdown of symmetry in the folding transition state of protein L
17. Critical role of beta-hairpin formation in protein G folding
18. Native protein sequences are close to optimal for their structures
19. Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding
20. Stabilisation of alpha-helices by site-directed mutagenesis reveals the importance of secondary structure in the transition state for acylphosphatase folding
21. From snapshot to movie: Phi analysis of protein folding transition states taken one step further
22. The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved
23. Obligatory steps in protein folding and the conformational diversity of the transition state
24. Long-range order in the src SH3 folding transition state
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27. Three-dimensional solution structure of PsaE from the cyanobacterium Synechococcus sp. strain PCC 7002, a photosystem I protein that shows structural homology with SH3 domains
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29. 7 chaperonin complex
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32. Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL
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35. GroEL-GroES cycling: ATP and nonnative polypeptide direct alternation of folding-active rings
36. Catalysis of amide proton exchange by the molecular chaperones GroEL and SecB
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38. Significant hydrogen exchange protection in GroEL-bound DHFR is maintained during iterative rounds of substrate cycling
39. Native-like structure of a protein-folding intermediate bound to the chaperonin GroEL
40. Chaperonin function: Folding by forced unfolding
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42. Two conformational states of beta-lactamase bound to GroEL: A biophysical characterization
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44. A thermodynamic coupling mechanism for GroEL-mediated unfolding
45. The chaperonin GroEL binds to late-folding non-native conformations present in native Escherichia coli and murine dihydrofolate reductases
46. A thermodynamic coupling mechanism can explain the GroEL-mediated acceleration of the folding of barstar
47. Chaperonins can catalyse the reversal of early aggregation steps when a protein misfolds
48. Multivalent binding of nonnative substrate proteins by the chaperonin GroEL
49. The crystal structure of a GroEL/peptidecomplexplasticity as a basis for substrate diversity
50. Residues in chaperonin GroEL required for polypeptide binding and release
51. A structural model for GroEL-polypeptide recognition
52. The chaperonin GroEL binds a polypeptide in an alpha-helical conformation
53. NMR analysis of the binding of a rhodanese peptide to a minichaperone in solution
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55. Secondary structure forming propensity coupled with amphiphilicity is an optimal motif in a peptide or protein for association with chaperonin 60 (GroEL)
56. Identification of in vivo substrates of the chaperonin GroEL
57. GroEL accelerates the refolding of hen lysozyme without changing its folding mechanism
58. GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms
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60. Catalysis, commitment and encapsulation during GroE-mediated folding
61. Analysis of GroE-assisted folding under nonpermissive conditions
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64. Submillisecond folding of the peripheral subunit-binding domain
65. Cytochrome c folding triggered by electron transfer
66. Rapid folding with and without populated intermediates in the homologous four-helix proteins Im7 and Im9
67. The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP
68. Folding kinetics of villin 14T, a protein domain with a central beta-sheet and two hydrophobic cores
69. Global analysis of the effects of temperature and denaturant on the folding and unfolding kinetics of the N-terminal domain of the protein L9
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81. Different folding transition states may result in the same native structure
82. The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology
83. Folding of circular and permuted chymotrypsin inhibitor 2: Retention of the folding nucleus
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85. Structure of the transition state for folding of the 129 aa protein CheY resembles that of a smaller protein, CI-2
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88. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
89. The SH3-fold family: Experimental evidence and prediction of variation in the folding pathways