By S. L. Bonting, F. J. M. Daemen (auth.), Professor Dr. L. Jaenicke (eds.)
This quantity includes the complaints of the twenty fifth Mosbach Colloquium, the final subject matter of that's the Biochemistry of Sensory services. It was once meant, carrying on with the silver-tradition of those Colloquia, to supply the uninitiated biochemist with an perception into the present prestige of a line of study in Molecular Biology which, greater than many different fields in Biochemistry, has maintained its contacts with and admire for body structure. The audio system have been requested to try to stipulate their subject sufficiently to outline the basics and to accumulate upon this foundation the extra subtle information in their personal stories. it's for the reader to guage how good either organizer and individuals 1 have attained this finish • those lawsuits not just replicate the hubs round which numerous teams of scientists wheel yet can also function a resource of literature references and for the complicated pupil as an advent to this hugely updated department of Biochemistry, even if no index is supplied because the desk of con tents is taken into account enough to find lots of the s,
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Additional info for Biochemistry of Sensory Functions
2) . During the meta I-II transition a conformation-change takes place in which a base is exposed (Mn*). This "unfolded" conformation is stabilized by protonation, since the proton is too polar to be re-enfolded into the hydrophobic core of metarhodopsin. Mrr* and MnH+ are assumed to have similar spectra. 005). The pH-dependence results from the second equilibrium, characterized by the association-constant of the exposed base KB == [MnH+]f[H+] [Mn*] ~ 108 •5 • At low temperature only increasing proton-concentrations shift the equilibrium to meta II by stabilizing MnH+ (down to pH 6; higher proton-concentrations appear to induce partial denaturation; on the other hand in the alkaline a Mn-similar substance is stabilized).
Nat. Acad. Sci. ) 68, 713 (1971). : Vision Res. 12, 1697 (1972). : Biochim. biophys. ) 303, 189 (1973a). : Biochim. biophys. ) 323, 125 (1973b). : Biochim. biophys. ) 321), 315 (1973c). : Ann. Rev. Biophys. 1, 131 (1972). : Trans. Faraday Soc. 27, 180 (1959). : J. molec. Biol. 41), 397 (1969). : Biochemistry I, 2914 (1968). : Biochim. biophys. ) 341), 468 (1974). : J. gen. Physiol. 42, 259 (1958). : J. gen. Physiol. 36, 269 (1952). : Exp. Eye Res. 16, 343 (1973). : J. gen. Physiol. 60,20 (1972).
Vertebrate visual pigments can be regenerated in vitro by mixing opsin with ll-cis-retinaI. It is generally assumed that in vivo ll-cis-retinalis drawn from the ocular stores of all-trans-vitamin A esters. The sequence and precise mechanisms of the reactions by which the esters are hydrolyzed, oxidized and isomerized to ll-cisretinal are not yet clear. The only way in which invertebrate rhodopsin has been regenerated in vitro is by photoisomerization of the chromophores ofbatho-, lumi- ormetarhodopsin (cf.
Biochemistry of Sensory Functions by S. L. Bonting, F. J. M. Daemen (auth.), Professor Dr. L. Jaenicke (eds.)