Abstract
Nuclear magnetic resonance (NMR) has become the first technique applicable for determination of three-dimensional biopolymer structures in solution and other noncrystalline states. Comparable data have so far been obtained exclusively by X-ray diffraction in single crystals. This article presents a brief survey of NMR assignments and structure determination with proteins, and some initial implications on the state of proteins in solution are discussed.KeywordsNuclear Magnetic ResonanceCross PeakGlobular ProteinResonance AssignmentDistance ConstraintThese keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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