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The sequences of small proteins are not extensively optimized for rapid folding by natural selection

Author

David Baker

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

Date of publication: April 1, 1998

Language: English

Main subject: protein folding

Bibliographic databases:

Cites articles 16

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Title

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Are there pathways for protein folding?
September 15, 1992

Protein folding funnels: a kinetic approach to the sequence-structure relationship
August 1, 1993

Catalysis of a protein folding reaction: thermodynamic and kinetic analysis of subtilisin BPN' interactions with its propeptide fragment
August 1, 1993

Engineering of stable and fast-folding sequences of model proteins
April 1, 1993

Proton nuclear magnetic resonance sequential assignments and secondary structure of an immunoglobulin light chain-binding domain of protein L
June 1, 1994

Kinetics versus thermodynamics in protein folding
March 1995

Funnels, pathways, and the energy landscape of protein folding: a synthesis
July 1, 1995

Mapping of the Immunoglobulin Light Chain-binding Site of Protein L
June 1, 1995

A phage display system for studying the sequence determinants of protein folding
June 1, 1996

Direct evidence for a two-state protein unfolding transition from hydrogen-deuterium exchange, mass spectrometry, and NMR.
December 1, 1997

Contrasting roles for symmetrically disposed beta-turns in the folding of a small protein
October 1, 1997

Functional rapidly folding proteins from simplified amino acid sequences
June 1, 1997

Transient aggregates in protein folding are easily mistaken for folding intermediates
January 1997

From Levinthal to pathways to funnels
March 1997

Kinetics of Folding of the IgG Binding Domain of Peptostreptoccocal Protein L
January 1, 1997

Strain in the folding nucleus of chymotrypsin inhibitor 2

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