Kinetic analysis of molecular dynamics simulations reveals changes in the denatured state and switch of folding pathways upon single-point mutation of a β-sheet miniprotein

Proteins: Structure, Function and Genetics

Volumn 70, Issue 4, 2008, Pages 1185-1195

  Muff, Stefanie ^a   Caflisch, Amedeo ^a  

^a UNIVERSITY OF ZURICH   (Switzerland)

Author keywords

Complex network; Free energy surface; Multiple folding pathways; Non native interactions; Transition state

Indexed keywords

PROTEIN;

ARTICLE; BETA SHEET; ENERGY TRANSFER; HYDROPHOBICITY; MOLECULAR DYNAMICS; POINT MUTATION; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; TEMPERATURE DEPENDENCE; THERMODYNAMICS;

COMPUTER SIMULATION; KINETICS; MOTION; POINT MUTATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY;

EID: 39749156392     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21565     Document Type: Article

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