A pathway for the thermal destabilization of bacteriorhodopsin

Stefka G. Taneva, JoséM M.M. Caaveiro, Arturo Muga, Félix M. Goñi

Research output: Contribution to journalArticle

44 Citations (Scopus)

Abstract

A variety of structural techniques, including IR spectroscopy, reveals that thermal denaturation of bacteriorhodopsin follows a given pathway (successively rearrangement of helical structures, extensive deuterium exchange, and finally protein aggregation) irrespective of heating rate, pH or ionic strength conditions. In all cases, thermal denaturation leads to a 'compact denatured state' which retains a large proportion of ordered structure.

Original languageEnglish
Pages (from-to)297-300
Number of pages4
JournalFEBS Letters
Volume367
Issue number3
DOIs
Publication statusPublished - Jul 3 1995

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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