A PATHWAY FOR THE THERMAL DESTABILIZATION OF BACTERIORHODOPSIN

Citation
Sg. Taneva et al., A PATHWAY FOR THE THERMAL DESTABILIZATION OF BACTERIORHODOPSIN, FEBS letters, 367(3), 1995, pp. 297-300
Citations number
19
Categorie Soggetti
Biophysics,Biology
Journal title
ISSN journal
00145793
Volume
367
Issue
3
Year of publication
1995
Pages
297 - 300
Database
ISI
SICI code
0014-5793(1995)367:3<297:APFTTD>2.0.ZU;2-K
Abstract
A variety of structural techniques, including IR spectroscopy, reveals that thermal denaturation of bacteriorhodopsin follows a given pathwa y (successively rearrangement of helical structures, extensive deuteri um exchange, and finally protein aggregation) irrespective of heating rate, pH or ionic strength conditions, In all cases, thermal denaturat ion leads to a 'compact denatured state' which retains a large proport ion of ordered structure.