Direct measurement of salt-bridge solvation energies using a peptide model system: Implications for protein stability

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

Volumn 93, Issue 7, 1996, Pages 2985-2990

  Wimley, W C ^a   Gawrisch, K ^a   Creamer, T P ^a   White, S H ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

13C NMR; electrostatics; hydrophobicity; octanol partitioning; protein folding

Indexed keywords

OCTANOL; PENTAPEPTIDE;

ARTICLE; CARBON NUCLEAR MAGNETIC RESONANCE; ENERGY TRANSFER; HYDROPHOBICITY; MOLECULAR MODEL; PEPTIDE SYNTHESIS; PRIORITY JOURNAL; PROTEIN FOLDING; SOLVATION; SYSTEM ANALYSIS;

AMINO ACID SEQUENCE; AMINO ACIDS; BUFFERS; CALORIMETRY; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; HYDROGEN-ION CONCENTRATION; KINETICS; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; OLIGOPEPTIDES; PROTEIN CONFORMATION; SALTS; SOLUBILITY; SPECTROMETRY, MASS, FAST ATOM BOMBARDMENT; STRUCTURE-ACTIVITY RELATIONSHIP; THERMODYNAMICS;

EID: 0029864591     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.93.7.2985     Document Type: Article

References (0)