(Q73174236)

English

Monte Carlo simulations of protein folding using inexact potentials: how accurate must parameters be in order to preserve the essential features of the energy landscape?

scientific article published on 01 January 1996

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scholarly article

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1 November 2019

Monte Carlo simulations of protein folding using inexact potentials: how accurate must parameters be in order to preserve the essential features of the energy landscape? (English)

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1 November 2019

energy landscape

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author name string

Pereira de Araújo AF

1

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1 November 2019

Pochapsky TC

2

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publication date

1 January 1996

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1 November 2019

Folding & design

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1 November 2019

1

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1 November 2019

299-314

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1 November 2019

4

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1 November 2019

Theoretical studies of protein folding and unfolding

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Towards protein folding by global energy optimization

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A simplified representation of protein conformations for rapid simulation of protein folding

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Folding protein alpha-carbon chains into compact forms by Monte Carlo methods

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Simulations of the folding of a globular protein.

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Monte Carlo simulations of protein folding. II. Application to protein A, ROP, and crambin

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A computer model to dynamically simulate protein folding: studies with crambin.

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Equation of State Calculations by Fast Computing Machines

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Dynamic Monte Carlo simulations of a new lattice model of globular protein folding, structure and dynamics

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Monte Carlo simulations of protein folding. I. Lattice model and interaction scheme.

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How does a protein fold?

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Protein folding funnels: a kinetic approach to the sequence-structure relationship

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Calculation of conformational ensembles from potentials of mean force. An approach to the knowledge-based prediction of local structures in globular proteins.

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A chromatographic approach to the determination of relative free energies of interaction between hydrophobic and amphiphilic amino acid side chains

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Perfect temperature for protein structure prediction and folding.

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Proteins with selected sequences fold into unique native conformation

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Engineering of stable and fast-folding sequences of model proteins

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Optimal protein-folding codes from spin-glass theory

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

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Evolution-like selection of fast-folding model proteins

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A new approach to the design of stable proteins

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Formation of unique structure in polypeptide chains. Theoretical investigation with the aid of a replica approach

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Spin glasses and the statistical mechanics of protein folding

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Funnels, pathways, and the energy landscape of protein folding: a synthesis

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Toward an outline of the topography of a realistic protein-folding funnel

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Principles of protein folding--a perspective from simple exact models.

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Impact of local and non-local interactions on thermodynamics and kinetics of protein folding

1 reference

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Identifiers

10.1016/S1359-0278(96)00043-0

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Europe PubMed Central

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1 November 2019

1 reference

Europe PubMed Central

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1 November 2019

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