By Gerald Litwack
Lower than the able and certified editorial management of Dr. Gerald Litwack, supplementations and Hormones keeps to submit state of the art experiences of curiosity to endocrinologists, biochemists, nutritionists, pharmacologists, mobile biologists, and molecular biologists. First released in 1943, supplementations and Hormones is the longest-running serial released by way of educational Press. within the early days of the Serial, the themes of supplementations and hormones have been fairly unique. Now, new discoveries have proved that numerous of the supplements functionality as hormones and plenty of of the elements inferred via the identify of the serial functionality in sign transduction approaches. as a result, the Editor-in-Chief has accelerated the scope of the serial to mirror this more recent realizing of function-structure relationships in mobile conversation. The Editorial Board now displays services within the box of hormone motion, diet motion, X-ray crystal constitution, body structure, and enzyme mechanisms.
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Extra info for Advances in Research and Applications
Biophys. J. 2, 161-178. Lin, S. , and Sakmar, T. P. (1996). Specific tryptophan UV-absorbance changes are probes of the transition of rhodopsin to its active state. Biochemistry 35, 1114911159. Mathews, R. , and Wald, G. (1963). Tautomeric forms of metarhodopsin. J. Gen. Physiol. 47, 215-240. Mierke, D. , and Chorev, M. (1996). Third cytoplasmic loop of the PTH/PTHrP receptor. J. Am. Chem. Sot. 118,8998-9004. Mitchell, D. , and Litman, B. J. (19901. Modulation of metarhodopsin formation by cholesterol-induced ordering of bilayers.
Inclusion of these residues allowed unambiguous docking of the carboxyl-terminal domain to a model of the a-helix of the transmembrane domain. The structure of the carboxyl-terminal domain (in addition to structures of other domains) is shown in Fig. 4. Several interesting observations can be made. Residues that were not predicted to be a-helical by 40 ARLENE D. ALBERT FIG. 4. Three-dimensional structures terminus, and one of the transmembrane solution NMR. AND of peptides helices PHILIP L. YEAGLE corresponding to loops, C terminus, of bovine rhodopsin as determined N by hydropathy analysis exhibit o-helical structure.
Tautomeric forms of metarhodopsin. J. Gen. Physiol. 47, 215-240. Mierke, D. , and Chorev, M. (1996). Third cytoplasmic loop of the PTH/PTHrP receptor. J. Am. Chem. Sot. 118,8998-9004. Mitchell, D. , and Litman, B. J. (19901. Modulation of metarhodopsin formation by cholesterol-induced ordering of bilayers. Biochemistry 29,9143-9149. Mitchell, D. , and Litman, B. J. (1991). Rhodopsin in dimyristoylphosphatidylcholine-reconstituted bilayers forms matarhodopsin II and activates Gt. Biochemistry 30,37-42.