(Q58882364)

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Folding and misfolding of designed proteinlike chains with mutations

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Folding and misfolding of designed proteinlike chains with mutations (English)

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G. Tiana

1

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R. A. Broglia

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2

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H. E. Roman

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3

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E. Vigezzi

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4

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E. Shakhnovich

series ordinal

5

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language of work or name

English

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publication date

8 January 1998

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published in

Journal of Chemical Physics

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volume

108

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page(s)

757-761

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issue

2

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cites work

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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retrieved

21 January 2018

Implications of thermodynamics of protein folding for evolution of primary sequences

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reference URL

https://api.crossref.org/works/10.1063%2F1.475435

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21 January 2018

Engineering of stable and fast-folding sequences of model proteins

1 reference

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reference URL

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21 January 2018

Specific nucleus as the transition state for protein folding: evidence from the lattice model.

1 reference

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reference URL

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retrieved

21 January 2018

Conserved residues and the mechanism of protein folding

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reference URL

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21 January 2018

Evolution-like selection of fast-folding model proteins

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reference URL

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21 January 2018

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

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reference URL

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retrieved

21 January 2018

Optimal protein-folding codes from spin-glass theory

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reference URL

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retrieved

21 January 2018

Influence of point mutations on protein structure: probability of a neutral mutation

1 reference

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reference URL

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retrieved

21 January 2018

Protein folding bottlenecks: A lattice Monte Carlo simulation

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21 January 2018

Criterion that determines the foldability of proteins

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reference URL

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retrieved

21 January 2018

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(Q58882364)

Folding and misfolding of designed proteinlike chains with mutations

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