Low-populated folding intermediates of Fyn SH3 characterized by relaxation dispersion NMR. (Q30163903)

9 June 2017

Low-populated folding intermediates of Fyn SH3 characterized by relaxation dispersion NMR. (English)

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9 June 2017

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Ariel A Di Nardo

4

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Xavier Salvatella

object named as

Xavier Salvatella

series ordinal

2

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Lewis E. Kay

series ordinal

7

object named as

Lewis E Kay

1 reference

9 June 2017

3

Michele Vendruscolo

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9 June 2017

6

Christopher M Dobson

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9 June 2017

Dmitry M Korzhnev

1

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9 June 2017

Alan R Davidson

series ordinal

5

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9 June 2017

language of work or name

English

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publication date

1 July 2004

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9 June 2017

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430

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6999

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9 June 2017

586-590

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The kinetic pathway of folding of barnase

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Hammond behavior versus ground state effects in protein folding: evidence for narrow free energy barriers and residual structure in unfolded states.

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Long-range interactions within a nonnative protein

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Protein folding and misfolding

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The present view of the mechanism of protein folding

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Hydrophobic core packing in the SH3 domain folding transition state

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The folding kinetics and thermodynamics of the Fyn-SH3 domain.

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The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved.

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Long-range order in the src SH3 folding transition state

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Dramatic acceleration of protein folding by stabilization of a nonnative backbone conformation

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Studying excited states of proteins by NMR spectroscopy.

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Win some, lose some: enthalpy-entropy compensation in weak intermolecular interactions

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Three key residues form a critical contact network in a protein folding transition state

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Probing multiple effects on 15N, 13C alpha, 13C beta, and 13C' chemical shifts in peptides using density functional theory

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Protein folding kinetics beyond the phi value: using multiple amino acid substitutions to investigate the structure of the SH3 domain folding transition state

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Mutagenesis of a buried polar interaction in an SH3 domain: sequence conservation provides the best prediction of stability effects.

21 January 2018

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Slow dynamics in folded and unfolded states of an SH3 domain

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Determination of a transition state at atomic resolution from protein engineering data

21 January 2018

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How do small single-domain proteins fold?

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Negative activation enthalpies in the kinetics of protein folding

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Protein Folding: A Perspective from Theory and Experiment.

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The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data

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Identifiers

DOI

10.1038/NATURE02655

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Dimensions Publication ID

9 June 2017

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