TY - JOUR
T1 - The role of water in retinal complexation to bacterio-opsin
AU - Rousso, Itay
AU - Brodsky, Igor
AU - Lewis, Aaron
AU - Sheves, Mordechai
PY - 1995/6/9
Y1 - 1995/6/9
N2 - A system is described that allows for the delineation of the factors that effect the complexation of retinal to the apoprotein of bacteriorhodopsin. This complexation is investigated in various states of hydration, in H2O and D2O, at a variety of pH levels, with mutant membranes and labeled retinals. The complexation reaction was also investigated using absorption spectroscopy and vibrational spectra using difference Fourier transform infrared spectroscopy. The results demonstrate the crucial role of water in controlling the protein conformations that lead to protein/ligand binding reactions and begin to shed new light on the protein control of a reaction that normally cannot take place in an aqueous medium.
AB - A system is described that allows for the delineation of the factors that effect the complexation of retinal to the apoprotein of bacteriorhodopsin. This complexation is investigated in various states of hydration, in H2O and D2O, at a variety of pH levels, with mutant membranes and labeled retinals. The complexation reaction was also investigated using absorption spectroscopy and vibrational spectra using difference Fourier transform infrared spectroscopy. The results demonstrate the crucial role of water in controlling the protein conformations that lead to protein/ligand binding reactions and begin to shed new light on the protein control of a reaction that normally cannot take place in an aqueous medium.
UR - http://www.scopus.com/inward/record.url?scp=0029017477&partnerID=8YFLogxK
U2 - 10.1074/jbc.270.23.13860
DO - 10.1074/jbc.270.23.13860
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C2 - 7775444
AN - SCOPUS:0029017477
SN - 0021-9258
VL - 270
SP - 13860
EP - 13868
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 23
ER -