A pathway for the thermal destabilization of bacteriorhodopsin

Stefka G. Taneva, Jose Manuel Martinez 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

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Bacteriorhodopsins
Denaturation
Hot Temperature
Deuterium
Ionic strength
Heating rate
Osmolar Concentration
Heating
Infrared spectroscopy
Spectrum Analysis
Agglomeration
Proteins

All Science Journal Classification (ASJC) codes

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

Cite this

A pathway for the thermal destabilization of bacteriorhodopsin. / Taneva, Stefka G.; Martinez Caaveiro, Jose Manuel; Muga, Arturo; Goñi, Félix M.

In: FEBS Letters, Vol. 367, No. 3, 03.07.1995, p. 297-300.

Research output: Contribution to journalArticle

Taneva, Stefka G. ; Martinez Caaveiro, Jose Manuel ; Muga, Arturo ; Goñi, Félix M. / A pathway for the thermal destabilization of bacteriorhodopsin. In: FEBS Letters. 1995 ; Vol. 367, No. 3. pp. 297-300.
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