Residual dipolar couplings measured in unfolded proteins are sensitive to amino-acid-specific geometries as well as local conformational sampling

Biochemical Society Transactions

Volumn 40, Issue 5, 2012, Pages 989-994

  Huang, Jie Rong ^a   Gentner, Martin ^b   Vajpai, Navratna ^b   Grzesiek, Stephan ^b   Blackledge, Martin ^a  

^a INSTITUT DE BIOLOGIE STRUCTURALE   (France)

^b UNIVERSITY OF BASEL   (Switzerland)

Author keywords

Coil library; Flexible Meccano algorithm; Intrinsically disordered protein (IDP); Molecular dynamics simulation; Residual dipolar coupling (RDC); Statistical coil model

Indexed keywords

AMINO ACID;

ALGORITHM; CIS TRANS ISOMERISM; ENERGY; EXPERIMENTAL STUDY; GEOMETRY; MOLECULAR MODEL; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN STRUCTURE; PROTEIN UNFOLDING; RESIDUAL DIPOLAR COUPLING; REVIEW; SIMULATION; SPIN LABELING; STATISTICAL MODEL;

ALGORITHMS; AMINO ACIDS; COMPUTATIONAL BIOLOGY; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN CONFORMATION; PROTEIN UNFOLDING; PROTEINS;

EID: 84866645524     PISSN: 03005127     EISSN: 14708752     Source Type: Journal    
DOI: 10.1042/BST20120187     Document Type: Review

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