Structure and disorder in the ribonuclease S-peptide probed by NMR residual dipolar couplings

Protein Science

Volumn 12, Issue 10, 2003, Pages 2132-2140

  Alexandrescu, Andrei T ^a   Kammerer, Richard A ^b  

^a UNIVERSITY OF CONNECTICUT   (United States)

^b UNIVERSITY OF MANCHESTER   (United Kingdom)

Author keywords

Alignment in liquid crystals; Denatured state; Protein dynamics; Protein folding; RDC

Indexed keywords

OCTANOL; RIBONUCLEASE A; SODIUM CHLORIDE;

ANISOTROPY; ARTICLE; CRYSTAL STRUCTURE; DENATURATION; DIPOLE; DYNAMICS; DYNAMOMETRY; ENZYME STRUCTURE; HYDROPHOBICITY; LIQUID; LOW TEMPERATURE PROCEDURES; MOLECULAR STABILITY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN STRUCTURE; SIMULATION;

1-OCTANOL; ALGORITHMS; ANISOTROPY; AUTOMATIC DATA PROCESSING; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; NITROGEN ISOTOPES; OSMOLAR CONCENTRATION; PEPTIDE FRAGMENTS; POLYETHYLENE GLYCOLS; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT FUSION PROTEINS; RIBONUCLEASE, PANCREATIC; TEMPERATURE;

EID: 0141747176     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.03164403     Document Type: Article

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