DETERMINATION OF PROTEIN STRUCTURES BY NMR-APPROACHES TOWARDS EXTENDING THE LIMITS

Abstract

Nuclear magnetic resonance spectroscopy has evolved into a powerful technique for structure determination in solution. Key advances have been the introduction of two dimensional experiments, high field superconducting magnets and computational proceedures for converting the experimental data into three-dimensional structures. Present attempts to extendthe limits of the approach, both with respectto the molecular weight range of molecules that can be studied, as wellasto the precision with whichthosestructures can be obtained are discussed.