Structural dynamics of proteins, scaling behaviour and liquid glass transition

W. Doster, S. Cusack, W. Petry

Research output: Contribution to journalArticlepeer-review

8 Scopus citations

Abstract

Inelastic neutron scattering was used to study liquid-like motions and the nature of a dynamical transition in myoglobin, a small globular protein. The signature of the transition is a strong enhancement of low-frequency density fluctuations and a corresponding non-linear increase in atomic mean squared displacement above 180 K. The inelastic scattering function displays two power-law regions, whereby the crossover energy decreases with temperature. It is shown that the rescaled spectrum approximates a temperature and wave vector independent master function. Such features have been predicted for simple undercooled liquids in the vicinity of the glass transition by recent mode coupling theories.

Original languageEnglish
Pages (from-to)357-361
Number of pages5
JournalJournal of Non-Crystalline Solids
Volume131-133
Issue numberPART 1
DOIs
StatePublished - 11 Jun 1991
Externally publishedYes

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