NMR Studies of Structure and Function of Biological Macromolecules (Nobel Lecture)

摘要

Nuclear magnetic resonance (NMR) spectroscopy is unique among the methods available for three-dimensional structure determination of proteins and nucleic acids at atomic resolution, since the NMR data can be recorded in solution. Considering that body fluids such as blood, stomach liquid, and saliva are protein solutions where these molecules perform their physiological functions, knowledge of the molecular structures in solution is highly relevant. In the NMR experiments, solution conditions such as the temperature, pH, and salt concentration can be adjusted so as to closely mimic a physiological fluid. Conversely, the solutions may also be changed to quite extreme nonphysiological conditions, for example, for studies of protein denaturation. Furthermore, in addition to protein structure determination, NMR applications include investigations of dynamic features of the molecular structures, as well as studies of structural, thermodynamic, and kinetic aspects of interactions between proteins and other solution components, which may either be other macromolecules or low-molecular-weight ligands. Again, for these supplementary data it is of keen interest that they can be measured directly in solution.