Annu. Rev. Biophys. Biomol. Struct. 1999. 28:235–68 Copyright c  1999 by Annual Reviews. All rights reserved SOLID-STATE NUCLEAR MAGNETIC RESONANCE INVESTIGATION OF PROTEIN AND POLYPEPTIDE STRUCTURE Riqiang Fu 1 and Timothy A. Cross 1,2 1 Center for Interdisciplinary Magnetic Resonance at the National High Magnetic Field Laboratory and 2 Department of Chemistry, Institute of Molecular Biophysics, Florida State University, Tallahassee, Florida 32310; e-mail: rfu@magnet.fsu.edu, cross@magnet.fsu.edu KEY WORDS: orientational constraints, oriented samples, distance constraints, magic angle spinning, torsional constraints ABSTRACT Solid-state nuclear magnetic resonance (NMR) is rapidly emerging as a suc- cessful and important technique for protein and peptide structural elucidation from samples in anisotropic environments. Because of the diversity of nuclei and nuclear spin interactions that can be observed, and because of the broad range of sample conditions that can be studied by solid-state NMR, the poten- tial for gaining structural constraints is great. Structural constraints in the form of orientational, distance, and torsional constraints can be obtained on proteins in crystalline, liquid-crystalline, or amorphous preparations. Great progress in the past few years has been made in developing techniques for obtaining these constraints, and now it has also been clearly demonstrated that these constraints can be assembled into uniquely defined three-dimensional structures at high res- olution. Although much progress toward the development of solid-state NMR as a routine structural tool has been documented, the future is even brighter with the continued development of the experiments, of NMR hardware, and of the molecular biological methods for the preparation of labeled samples. 235 1056-8700/99/0610-0235$08.00 Annu. Rev. Biophys. Biomol. Struct. 1999.28:235-268. Downloaded from arjournals.annualreviews.org by Florida State University on 04/10/07. For personal use only.