Coupled motion in proteins revealed by pressure perturbation

Yinan Fu, Vignesh Kasinath, Veronica R. Moorman, Nathaniel V. Nucci, Vincent J. Hilser, A. Joshua Wand

Research output: Contribution to journalArticlepeer-review

69 Scopus citations

Abstract

The cooperative nature of protein substructure and internal motion is a critical aspect of their functional competence about which little is known experimentally. NMR relaxation is used here to monitor the effects of high pressure on fast internal motion in the protein ubiquitin. In contrast to the main chain, the motions of the methyl-bearing side chains have a large and variable pressure dependence. Within the core, this pressure sensitivity correlates with the magnitude of motion at ambient pressure. Spatial clustering of the dynamic response to applied hydrostatic pressure is also seen, indicating localized cooperativity of motion on the sub-nanosecond time scale and suggesting regions of variable compressibility. These and other features indicate that the native ensemble contains a significant fraction of members with characteristics ascribed to the recently postulated "dry molten globule". The accompanying variable side-chain conformational entropy helps complete our view of the thermodynamic architecture underlying protein stability, folding, and function.

Original languageEnglish (US)
Pages (from-to)8543-8550
Number of pages8
JournalJournal of the American Chemical Society
Volume134
Issue number20
DOIs
StatePublished - May 23 2012

All Science Journal Classification (ASJC) codes

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

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