TY - JOUR
T1 - A pathway for the thermal destabilization of bacteriorhodopsin
AU - Taneva, Stefka G.
AU - Caaveiro, JoséM M.M.
AU - Muga, Arturo
AU - Goñi, Félix M.
N1 - Funding Information:
AcknowledgmenTtsh:i s work was supported in part by Grant No.
Funding Information:
PB91/0441 from DGICYT and Grant No. UPV 042.310-EB from the University of the Basque Country. S.G.T. thanks the Basque Government for a post-doctoral studentship.
PY - 1995/7/3
Y1 - 1995/7/3
N2 - 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.
AB - 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.
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U2 - 10.1016/0014-5793(95)00570-Y
DO - 10.1016/0014-5793(95)00570-Y
M3 - Article
C2 - 7607327
AN - SCOPUS:0029032977
SN - 0014-5793
VL - 367
SP - 297
EP - 300
JO - FEBS Letters
JF - FEBS Letters
IS - 3
ER -