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The single helix in protein L is largely disrupted at the rate-limiting step in folding

Author

David Baker

Published in: Journal of Molecular Biology

Date of publication: December 1, 1998

Language: English

Main subject: protein folding

Bibliographic databases:

Cites articles 35

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Computed circular dichroism spectra for the evaluation of protein conformation
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Partition analysis and the concept of net rate constants as tools in enzyme kinetics,Partition analysis and concept of net rate constants as tools in enzyme kinetics
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Mapping the transition state and pathway of protein folding by protein engineering
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Dominant forces in protein folding
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Large differences in the helix propensities of alanine and glycine
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MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures
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The folding of an enzyme. III. Structure of the transition state for unfolding of barnase analysed by a protein engineering procedure
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The folding of an enzyme. I. Theory of protein engineering analysis of stability and pathway of protein folding
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Three-dimensional solution structure of an immunoglobulin light chain-binding domain of protein L. Comparison with the IgG-binding domains of protein G
April 1, 1994

Protein folding dynamics: the diffusion-collision model and experimental data
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An evolutionary approach to folding small alpha-helical proteins that uses sequence information and an empirical guiding fitness function
May 1, 1994

Helix propensities of the amino acids measured in alanine-based peptides without helix-stabilizing side-chain interactions

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Single versus parallel pathways of protein folding and fractional formation of structure in the transition state

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A phage display system for studying the sequence determinants of protein folding
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The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding

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Mapping of the Immunoglobulin Light Chain-binding Site of Protein L
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LINUS: a hierarchic procedure to predict the fold of a protein
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Fast events in protein folding: helix melting and formation in a small peptide
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Fast events in protein folding: relaxation dynamics of secondary and tertiary structure in native apomyoglobin
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The energy landscape of a fast-folding protein mapped by Ala-->Gly substitutions
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Laser temperature jump study of the helix<==>coil kinetics of an alanine peptide interpreted with a 'kinetic zipper' model,Laser Temperature Jump Study of the Helix⇌Coil Kinetics of an Alanine Peptide Interpreted with a ‘Kinetic Zipper' Model
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Kinetics of Folding of the IgG Binding Domain of Peptostreptoccocal Protein L
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Contrasting roles for symmetrically disposed beta-turns in the folding of a small protein
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Characterization of the free energy spectrum of peptostreptococcal protein L

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