th  - 1987 - 51st ENC Conference

WF32
SOLID STATE NMR OF PROTEINS
P. Stewart, R. McNamara, D. Chen, C. Lee, D. White, and S. Opella
Department of Chemistry
University of Pennsylvania
Philadelphia, Pennsylvania 19104
Recent results from solid state NMR studies of unoriented and oriented
protein samples will be presented. The analysis of powder pattern
lineshapes and relaxation parameters as a function of temperature is being
used to describe backbone and sidechain dynamics of proteins. A number
of different spectral parameters measured in oriented samples are being
interpreted in terms of structural parameters. In particular, a general
method for determining the mutual orientations of adjacent peptide planes
from solid state NMR measurements is being developed.
The spectroscopic experiments involve the observation of 13C, 15N and
14N resonances so that chemical shift, quadrupole, and dipole-dipole
interactions can be examined in multiple sites. The samples include
lysozyme, filamentous bacteriophage coat protein, and model peptides.