Tryptophan sidechain dynamics in hydrophobic oligopeptides determined by use of 13C nuclear magnetic resonance spectroscopy

This publication has 46 references indexed in Scilit:

• Sidechain rotational isomerization in proteins. Dynamic simulation with solvent surroundings
  Biophysical Journal, 1987
• Mixtures of a series of homologous hydrophobic peptides with lipid bilayers: a simple model system for examining the protein-lipid interface
  Biochemistry, 1986
• Effect of tryptophan derivatives on the phase properties of bilayers
  Biochimica et Biophysica Acta (BBA) - Biomembranes, 1985
• Carbon-13 NMR studies of the molecular dynamics of selectively carbon-13-enriched ribonuclease complexes
  Biochemistry, 1984
• Fluctuations in Protein Structure from X-Ray Diffraction
  Annual Review of Biophysics and Bioengineering, 1984
• pH-Induced conformational transitions of ferricytochrome c: a carbon-13 and deuterium nuclear magnetic resonance study
  Biochemistry, 1981
• Enzyme Dynamics: The Statistical Physics Approach
  Annual Review of Biophysics and Bioengineering, 1979
• Conformational studies on carbon-13-enriched human and bovine myelin basic protein, in solution and incorporated into liposomes
  Biochemistry, 1978
• Carbon-13 nuclear magnetic resonance spectroscopy of [2-¹³C]-carboxymethylcytochrome c
  Biochemistry, 1975
• Molecular aggregation in aqueous dispersions of phosphatidyl and lysophosphatidyl cholines
  Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1966