NMR and x‐ray studies show large movements within proteins
NOV 01, 1979
DOI: 10.1063/1.2995270
X‐ray crystallography provides information on the average structure of protein molecules. The images of atoms have always been broadened, but until the last few years this broadening was generally attributed to inaccuracies in the structure determination, lattice disorder and purely thermal vibration. Most crystallographers were skeptical about interpreting the temperature factors as structural motion. A typical small globular protein has a molecular weight of 20 000 a.m.u. and a diameter of 30–40 Å.
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© 1979 American Institute of Physics
