Identification of slow correlated motions in proteins using residual dipolar and hydrogen-bond scalar couplings

Proceedings of the National Academy of Sciences of the United States of America

Volumn 102, Issue 39, 2005, Pages 13885-13890

  Bouvignies, Guillaume ^a   Bernadó, Pau ^a   Meier, Sebastian ^d   Cho, Kyuil ^b   Grzesiek, Stephan ^d   Brüschweiler, Rafael ^c   Blackledge, Martin ^a  

^a CNRS   (France)

^b CLARK UNIVERSITY   (United States)

^c FLORIDA STATE UNIVERSITY   (United States)

^d UNIVERSITY OF BASEL   (Switzerland)

Author keywords

Correlated; Protein dynamics; Slow motions

Indexed keywords

AMINO ACID;

ALPHA HELIX; ARTICLE; BETA SHEET; DIPOLE; HYDROGEN BOND; HYDROPHOBICITY; MOLECULAR DYNAMICS; MOTION; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN INTERACTION; STATISTICAL MODEL;

AMINO ACIDS; BACTERIAL PROTEINS; HYDROGEN BONDING; HYDROPHOBICITY; MOTION; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN STRUCTURE, SECONDARY; PROTEINS;

EID: 25444532318     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.0505129102     Document Type: Article

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