A simple simulation model can reproduce the thermodynamic folding intermediate of apoflavodoxin

Proteins: Structure, Function and Bioinformatics

Volumn 78, Issue 1, 2010, Pages 73-82

  Larriva, María ^a   Prieto, Lidia ^a,c   Bruscolini, Pierpaolo ^b   Rey, Antonio ^a,b  

^a UNIVERSIDAD COMPLUTENSE DE MADRID   (Spain)

^b UNIVERSITY OF ZARAGOZA   (Spain)

^c CITY COLLEGE OF NEW YORK   (United States)

Author keywords

Free energy surface; Monte carlo; Populations; Protein folding; Topologybased models

Indexed keywords

APOFLAVODOXIN; FLAVODOXIN; UNCLASSIFIED DRUG; APOPROTEIN; BACTERIAL PROTEIN;

ANABAENA; ARTICLE; COMPUTER SIMULATION; CONFORMATIONAL TRANSITION; HISTOGRAM; MONTE CARLO METHOD; PRIORITY JOURNAL; PROTEIN FAMILY; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; THERMODYNAMICS; X RAY DIFFRACTION; CHEMICAL STRUCTURE; CHEMISTRY; PROTEIN CONFORMATION;

ANABAENA;

ANABAENA; APOPROTEINS; BACTERIAL PROTEINS; COMPUTER SIMULATION; FLAVODOXIN; MODELS, MOLECULAR; MONTE CARLO METHOD; PROTEIN CONFORMATION; PROTEIN FOLDING; THERMODYNAMICS;

EID: 77949352394     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22521     Document Type: Article

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