NMR characterization of partially folded and unfolded conformational ensembles of proteins

Biopolymers - Peptide Science Section

Volumn 51, Issue 3, 1999, Pages 191-207

  Barbar, Elisar ^a  

^a OHIO UNIVERSITY   (United States)

Author keywords

14 38 (Abu); Bovine pancreatic trypsin inhibitor; Hydrophobic core residues; Nmr; Protein ensembles; Selective labeling; Unfolded and partially folded proteins

Indexed keywords

CONFORMATIONS; ENZYME INHIBITION; HYDROPHOBICITY; MATHEMATICAL MODELS; MOLECULAR DYNAMICS; MOLECULES; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PHASE EQUILIBRIA; PROBES; STRUCTURE (COMPOSITION); SYNTHESIS (CHEMICAL);

BOVINE PANCREATIC TRYPSIN INHIBITOR; HYDROPHOBIC CORE RESIDUES; POLYPEPTIDE CHAIN;

PROTEINS;

APROTININ; POLYPEPTIDE; PROTEIN;

ARTICLE; HYDROPHOBICITY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE;

ANIMALS; APROTININ; CATTLE; HYDROGEN; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; NITROGEN ISOTOPES; PEPTIDE FRAGMENTS; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEINS; THERMODYNAMICS;

BOVINAE;

EID: 0032735941     PISSN: 00063525     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0282(1999)51:3<191::AID-BIP3>3.0.CO;2-B     Document Type: Article

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