| Literature DB >> 7607327 |
S G Taneva1, J M Caaveiro, A Muga, F M Goñi.
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.Entities:
Mesh：
Substances：
Year: 1995 PMID： 7607327 DOI： 10.1016/0014-5793(95)00570-y
Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124