Temperature-dependent X-ray diffraction as a probe of protein structural dynamics.

H Frauenfelder; G A Petsko; D Tsernoglou

doi:10.1038/280558a0

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Temperature-dependent X-ray diffraction as a probe of protein structural dynamics.

H Frauenfelder·G A Petsko·D Tsernoglou

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Abstract

X-ray diffraction at four temperatures from 220 to 300 K coupled with crystallographic refinement yields the mean-square displacements and conformational potentials of all 1,261 non-hydrogen atoms of metmyoglobin. The results are interpreted to indicate a condensed core around the haem, semi-liquid regions towards the outside and a possible pathway for ligands. It is concluded that X-ray diffraction can provide the spatial distribution of the dynamic features of a protein.

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Animals Ferric Compounds Motion Myoglobin Protein Conformation Temperature X-Ray Diffraction Journal Article Research Support, U.S. Gov't, Non-P.H.S.Research Support, U.S. Gov't, P.H.S.

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H Frauenfelder, G A Petsko, D Tsernoglou. 1979-08-16. Temperature-dependent X-ray diffraction as a probe of protein structural dynamics.. https://doi.org/10.1038/280558a0

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