Inter‐ and intramolecular motions in proteins

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The use of 57Fe Mössbauer radiation allows the study of protein crystal dynamics by a time‐resolved analysis of X‐ray scattering. In myoglobin cystals, the main source of the root mean squared amplitude of motions comes from intramolecular protein dynamics. Segments of the size of an α‐helix move collectively. Long‐range correlated motions give only a minor contribution. Comparison with Mössbauer absorption spectroscopy shows that protein‐specific dynamics is frozen out below 200 K and the lattice dynamics is mainly responsible for the low‐temperature behavior.

Original languageEnglish
Pages (from-to)1491-1498
Number of pages8
JournalInternational Journal of Quantum Chemistry
Issue number5
StatePublished - 5 Jun 1992
Externally publishedYes


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