Three-dimensional structures of proteins in solution by nuclear magnetic resonance spectroscopy.
Nuclear magnetic resonance (NMR) spectroscopy has emerged in recent years as a powerful method for the determination of three dimensional structures of small proteins in solution. Major cornerstones towards these advances were the introduction of two dimensional NMR experiments in combination with high field superconducting magnets, as well as the development of computational procedures to convert NMR derived distances into a 3D structure. This article outlines the methodology employed and illustrates its applicability based on a variety of examples.
Gronenborn
A M
AM
Max-Planck Institut für Biochemie, Martinsried bei München, Federal Republic of Germany.
Clore
G M
GM
D003198:Computer Simulation; D009682:Magnetic Resonance Spectroscopy; D011487:Protein Conformation; D012107:Research Design; D014961:X-Ray Diffraction