(Q44505970)

English

NMR and temperature-jump measurements of de novo designed proteins demonstrate rapid folding in the absence of explicit selection for kinetics

scientific article published in July 2003

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scholarly article

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Europe PubMed Central

3 December 2017

NMR and temperature-jump measurements of de novo designed proteins demonstrate rapid folding in the absence of explicit selection for kinetics (English)

1 reference

Europe PubMed Central

3 December 2017

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protein folding

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author name string

Blake Gillespie

1

1 reference

Europe PubMed Central

3 December 2017

Dung M Vu

2

1 reference

Europe PubMed Central

3 December 2017

Premal S Shah

3

1 reference

Europe PubMed Central

3 December 2017

Shannon A Marshall

4

1 reference

Europe PubMed Central

3 December 2017

R Brian Dyer

5

1 reference

Europe PubMed Central

3 December 2017

Stephen L Mayo

6

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Europe PubMed Central

3 December 2017

Kevin W Plaxco

7

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Europe PubMed Central

3 December 2017

language of work or name

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publication date

1 July 2003

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Europe PubMed Central

3 December 2017

Journal of Molecular Biology

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Europe PubMed Central

3 December 2017

330

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Europe PubMed Central

3 December 2017

4

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Europe PubMed Central

3 December 2017

813-819

1 reference

Europe PubMed Central

3 December 2017

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

1 reference

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How does a protein fold?

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Criterion that determines the foldability of proteins

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Buffed energy landscapes: another solution to the kinetic paradoxes of protein folding

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

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Functional rapidly folding proteins from simplified amino acid sequences.

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

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Conformational strain in the hydrophobic core and its implications for protein folding and design

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De novo protein design: fully automated sequence selection

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Energy functions for protein design

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Electrostatics significantly affect the stability of designed homeodomain variants

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Fast events in protein folding: helix melting and formation in a small peptide.

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Protein folding and unfolding in microseconds to nanoseconds by experiment and simulation

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Microsecond protein folding through a compact transition state

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Submillisecond folding of the peripheral subunit-binding domain 1 1Edited by P. E. Wright

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Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding

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Protein folding bottlenecks: A lattice Monte Carlo simulation

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Kinetics of protein folding. A lattice model study of the requirements for folding to the native state.

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Use of quantitative structure-property relationships to predict the folding ability of model proteins.

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How evolution makes proteins fold quickly

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Kinetics, thermodynamics and evolution of non-native interactions in a protein folding nucleus

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A protein engineering analysis of the transition state for protein folding: simulation in the lattice model

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Improved design of stable and fast-folding model proteins

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Kinetics and thermodynamics of folding of a de novo designed four-helix bundle protein

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Emergence of Preferred Structures in a Simple Model of Protein Folding

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Emergence of highly designable protein-backbone conformations in an off-lattice model.

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The topomer search model: A simple, quantitative theory of two-state protein folding kinetics

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Identifiers

10.1016/S0022-2836(03)00616-8

1 reference

Europe PubMed Central

3 December 2017

1 reference

Europe PubMed Central

3 December 2017

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