A structural model for unfolded proteins from residual dipolar couplings and small-angle x-ray scattering

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

Volumn 102, Issue 47, 2005, Pages 17002-17007

  Bernadó, Pau ^a   Blanchard, Laurence ^a   Timmins, Peter ^b   Marion, Dominique ^a   Ruigrok, Rob W H ^c   Blackledge, Martin ^a  

^a INSTITUT DE BIOLOGIE STRUCTURALE   (France)

^b INSTITUT LAUE LANGEVIN   (France)

^c CNRS   (France)

Author keywords

Conformational sampling; NMR; Protein dynamics; Protein folding; Random coil

Indexed keywords

PHOSPHOPROTEIN; PROTEIN; VIRUS PROTEIN;

AMINO ACID SEQUENCE; ARTICLE; MODEL; MOLECULAR DYNAMICS; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PARAINFLUENZA VIRUS 1; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DATABASE; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN STRUCTURE; QUANTITATIVE ANALYSIS; VIRUS NUCLEOCAPSID; X RAY CRYSTALLOGRAPHY;

MODELS, MOLECULAR; PHOSPHOPROTEINS; PROTEIN DENATURATION; PROTEIN STRUCTURE, TERTIARY; SCATTERING, RADIATION; SENDAI VIRUS; SEQUENCE ANALYSIS, PROTEIN; UREA; VIRAL PROTEINS; X-RAY DIFFRACTION; X-RAYS;

HUMAN PARAINFLUENZA VIRUS 1; SENDAI VIRUS;

EID: 28044458515     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.0506202102     Document Type: Article

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