Structure of the transition state for folding of the 129 aa protein CheY resembles that of a smaller protein, CI-2 (Q73174178)

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1 November 2019

title

Structure of the transition state for folding of the 129 aa protein CheY resembles that of a smaller protein, CI-2 (English)

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1 November 2019

author name string

E López-Hernández

series ordinal

1

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1 November 2019

L Serrano

series ordinal

2

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1 November 2019

publication date

1 January 1996

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1 November 2019

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1 November 2019

volume

1

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1 November 2019

issue

1

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1 November 2019

page(s)

43-55

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Characterizing transition states in protein folding: an essential step in the puzzle

1 November 2019

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The folding of an enzyme. IV. Structure of an intermediate in the refolding of barnase analysed by a protein engineering procedure

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The folding of an enzyme. II. Substructure of barnase and the contribution of different interactions to protein stability

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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. VI. The folding pathway of barnase: comparison with theoretical models

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Exploring the energy surface of protein folding by structure-reactivity relationships and engineered proteins: observation of Hammond behavior for the gross structure of the transition state and anti-Hammond behavior for structural elements for unfo

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Folding of chymotrypsin inhibitor 2. 2. Influence of proline isomerization on the folding kinetics and thermodynamic characterization of the transition state of folding

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Effect of cavity-creating mutations in the hydrophobic core of chymotrypsin inhibitor 2

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Structure of the hydrophobic core in the transition state for folding of chymotrypsin inhibitor 2: a critical test of the protein engineering method of analysis

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Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition

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Thermodynamic and kinetic analysis of the SH3 domain of spectrin shows a two-state folding transition.

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Kinetic analysis of folding and unfolding the 56 amino acid IgG-binding domain of streptococcal protein G.

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Extremely rapid protein folding in the absence of intermediates

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Evidence for a two-state transition in the folding process of the activation domain of human procarboxypeptidase A2.

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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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Three-dimensional structure of CheY, the response regulator of bacterial chemotaxis

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Magnesium binding to the bacterial chemotaxis protein CheY results in large conformational changes involving its functional surface

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Structural analysis of peptides encompassing all α-helices of three α/β parallel proteins: Che-Y, flavodoxin and P21-Ras: Implications for α-Helix stability and the folding of α/β parallel proteins

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Identifiers

DOI

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1 November 2019

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