Abstract
Saturation of single resonances in the proton nuclear magnetic resonance (NMR) spectrum of a protein in solution results in changes in intensities of other resonances. These changes come about either through nuclear Overhauser effects which arise because of dipolar coupling between the protons in the molecule, or through cross-saturation effects which arise when the protein fluctuates between different well defined conformations. For lysozyme from hen egg white (mol. wt. approx. 14,500) the method reveals details of the protein structure and of individual atom fluctuations.
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