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Long-range order in the src SH3 folding transition state

Author

David Baker

Published in: Proceedings of the National Academy of Sciences of the United States of America

Date of publication: June 1, 2000

Language: English

Main subject: SH3 domain

Bibliographic databases:

Cites articles 36

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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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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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Glutamine, alanine or glycine repeats inserted into the loop of a protein have minimal effects on stability and folding rates
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Important role of hydrogen bonds in the structurally polarized transition state for folding of the src SH3 domain
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Transition state in the folding of alpha-lactalbumin probed by the 6-120 disulfide bond,Transition state in the folding of α‐lactalbumin probed by the 6‐120 disulfide bond
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Folding of circular and permuted chymotrypsin inhibitor 2: retention of the folding nucleus,Folding of Circular and Permuted Chymotrypsin Inhibitor 2: Retention of the Folding Nucleus

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Experiment and theory highlight role of native state topology in SH3 folding
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Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding

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Transition state heterogeneity in GCN4 coiled coil folding studied by using multisite mutations and crosslinking
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The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP
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Contribution of a buried hydrogen bond to lambda repressor folding kinetics

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