Angular variances for internal bond rotations of side chains in GXG- based tripeptides derived from 13C-nmr relaxation measurements: Implications to protein folding

Biopolymers

Volumn 49, Issue 5, 1999, Pages 373-383

  Mikhailov, Dmitri V ^a   Washington, Lais ^a   Voloshin, Alexei M ^a   Daragan, Vladimir A ^a   Mayo, Kevin H ^a  

^a UNIVERSITY OF MINNESOTA   (United States)

Author keywords

13C nmr measurements; Angular variances; GXG based tripeptides; Internal bond rotations; Protein folding; Side chains

Indexed keywords

AMINO ACIDS; CHEMICAL BONDS; CONFORMATIONS; DIFFUSION; ENTROPY; HYDROPHOBICITY; MATHEMATICAL MODELS; MOLECULAR DYNAMICS; MOLECULAR STRUCTURE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEINS; RELAXATION PROCESSES;

LIPARI-SZABO MODEL FREE APPROACH; ROTATIONAL ANISOTROPIC DIFFUSION MODEL; ROTATIONAL JUMP MODEL;

POLYPEPTIDES;

TRIPEPTIDE;

AMINO ACID SEQUENCE; ARTICLE; CARBON NUCLEAR MAGNETIC RESONANCE; CHEMICAL BINDING; PROTEIN FOLDING; PROTEIN STRUCTURE; ROTATION;

EID: 0033561732     PISSN: 00063525     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0282(19990415)49:5<373::AID-BIP4>3.0.CO;2-V     Document Type: Article

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