Short-range, long-range and transition state interactions in the denatured state of ACBP from residual dipolar couplings

Journal of Molecular Biology

Volumn 339, Issue 5, 2004, Pages 1191-1199

  Fieber, Wolfgang ^a   Kristjansdottir, Sigridur ^a   Poulsen, Flemming M ^a  

^a UNIVERSITY OF COPENHAGEN   (Denmark)

Author keywords

ACBP; ACBP, acyl coenzyme A binding protein; denatured state; dipolar coupling; helix propensity; MFR, molecular fragment replacement; native like interaction; RDC, residual dipolar coupling

Indexed keywords

ALANINE; BINDING PROTEIN; HYDROGEN; ISOLEUCINE; NITROGEN; POLYACRYLAMIDE GEL; DIAZEPAM BINDING INHIBITOR;

ALPHA HELIX; ARTICLE; CHEMICAL BOND; COMPARATIVE STUDY; CONTROLLED STUDY; DATA ANALYSIS; DENATURATION; HYDROPHOBICITY; MUTATION; NONHUMAN; PH MEASUREMENT; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN ISOLATION; PROTEIN LOCALIZATION; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; SENSITIVITY ANALYSIS; SEQUENCE ANALYSIS; WILD TYPE; ANIMAL; CATTLE; CHEMICAL STRUCTURE; CHEMISTRY; METABOLISM; PROTEIN DENATURATION; PROTEIN SECONDARY STRUCTURE; SITE DIRECTED MUTAGENESIS;

BOVINAE;

ANIMALS; CATTLE; DIAZEPAM BINDING INHIBITOR; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY;

EID: 3042623821     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.04.037     Document Type: Article

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