(Q46016331)

18 December 2017

title

Folding rates and low-entropy-loss routes of two-state proteins. (English)

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18 December 2017

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2

Ken A Dill

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18 December 2017

author name string

Thomas R Weikl

series ordinal

1

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18 December 2017

language of work or name

English

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publication date

1 June 2003

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18 December 2017

Journal of Molecular Biology

published in

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18 December 2017

volume

329

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18 December 2017

issue

3

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18 December 2017

page(s)

585-598

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18 December 2017

Contact order, transition state placement and the refolding rates of single domain proteins.

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A possible folding pathway of bovine pancreatic RNase

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Constructing, verifying, and dissecting the folding transition state of chymotrypsin inhibitor 2 with all-atom simulations

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Stiffness of the distal loop restricts the structural heterogeneity of the transition state ensemble in SH3 domains

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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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7 January 2021

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7 January 2021

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A breakdown of symmetry in the folding transition state of protein L

7 January 2021

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The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology

7 January 2021

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Role of the chain termini for the folding transition state of the cold shock protein

7 January 2021

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Apparent two-state tendamistat folding is a sequential process along a defined route

7 January 2021

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10.1016/S0022-2836(03)00436-4

7 January 2021

Identifiers

DOI

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18 December 2017

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18 December 2017