Chapter 4 - Protein Structure Determination from NMR Data

Abstract

Significant progress is made in the past few years for determining protein structures from nD NMR data. Compared with the initial nuclear magnetic resonance (NMR) structures of ten years ago, the structures being determined today of much larger molecules are determined to higher precision and accuracy, and are being determined in much less time. NMR is seen now as being quite complementary to X-ray diffraction methods, and NMR structures are also being accepted by the general scientific community for being accurate structures, accounting for about 20% of the new structures determined during the past few years. Of obvious importance is the development of multichannel spectrometer hardware and indirect detection techniques. Other advances are because of continuing improvements in computer hardware and software, plus advances in techniques for calculating protein structures using NMR data. Besides the technology advances, there has been considerable growth in the number of people using NMR techniques to determine protein structure, as it is seen by the greatly increased attendance and number of posters and talks describing structure determinations at recent biological NMR conferences. Despite this growth, the field is still in its relative infancy. This chapter has the dual purpose of describing current problems and potential also. Some of the common methods are discussed, and the relative strengths and weaknesses of each method are presented.