An NMR study of the solution dynamics of deltorphin-I.
Nuclear spin relaxation rates associated with cross-correlated, dipole-dipole interactions are enlisted to help characterize the solution state dynamics of a small heptapeptide, deltorphin-I. A simple two-site jump model can be used to interpret the data obtained on two specific (13)C labeled residues, D-alanine and glycine. The influence of temperature and solvent upon the observed dynamics is investigated. Similarly, relaxation rates associated with dipole-shielding anisotropy interferences are used to examine the magnitude and orientation of various chemical shielding tensors within the D-alanine and glycine residues.
Chenon
Marie-Thérèse
MT
LADIR-CNRS, 2 rue Henry Dunant, 94320 Thiais, France.
Werbelow
Lawrence G
LG
D016880:Anisotropy; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D009842:Oligopeptides / Q000737:chemistry*; D011487:Protein Conformation; D012996:Solutions
D009842:Oligopeptides; D012996:Solutions; C060208:deltorphin I, Ala(2)-