Spotlights on Recent JACS Publications

摘要

Many important proteins in human biology resist structural analysis by X-ray crystallography and solution nuclear magnetic resonance (NMR) spectroscopy but are compatible with study by solid-state NMR. However, solid-state NMR comes with its own set of issues. While solution NMR provides information about the distances between hydrogen atoms in proteins, forming the basis for structure determination, in solid-state NMR signals from hydrogen atoms tend to overlap, making assignment and distance measurements difficult to attain. Markus Weingarth, Marc Baldus, and co-workers have developed a general approach for obtaining the side-chain proton contacts that define protein structure in solid-state NMR.