6] Determination of three-dimensional protein structures in solution by nuclear magnetic resonance: An overview

Abstract

Publisher Summary This chapter discusses the survey of the method, and describes more specialized contributions into perspective. Furthermore, the range of potential applications for the nuclear magnetic resonance (NMR) method of protein structure determination, and the type of results anticipated from it, are briefly discussed. At present, NMR is the only approach, besides diffraction techniques with single crystals, that is available for protein structure determination. Its introduction is of fundamental interest, because NMR can provide data that are in many ways complementary to those obtained from X-ray crystallography, and thus promises to widen the view of protein molecules for a better grasp of the relationships between structure and function. The method of protein structure determination by NMR involves several steps: data acquisition, spectral analysis, and structural interpretation of the experimental data. The NMR method is of prime interest for those working with polypeptides and proteins having molecular weights up to approximately 20,000. For molecules in this class the method provides stringent tests for the purity of the protein preparations the amino acid composition, and the amino acid sequence, and can yield a three-dimensional structure in solution at high resolution.