By George A. Jeffrey
ISBN-10: 0387508392
ISBN-13: 9780387508399
ISBN-10: 3540508392
ISBN-13: 9783540508397
Hydrogen bonds are susceptible points of interest, with a binding power under one-tenth that of a regular covalent bond. even though, hydrogen bonds are of amazing significance; with no all of them wood buildings may cave in, cement might fall apart, oceans may vaporize, and all dwelling issues may crumble into random dispersions of inert subject. Hydrogen Bonding in organic constructions is informative and eminently usable. it's, in a feeling, a Rosetta stone that unlocks a wealth of knowledge from the language of crystallography and makes it available to all scientists. (From a publication overview of Kenneth M. Harmon, technology 1992)
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Example text
Sci. A. 88, 11373 (1991). 13j. F. Moomaw and P. J. Casey, J. Biol. Chem. 267, 17438 (1992). 14y. Reiss, M. C. Seabra, M. S. Brown, and J. L. Goldstein, Biochem. Soc. Trans. 20, 487 (1992). [4] CHARACTERIZATION OF TYPE-n GGTase 23 tion. The assay is performed by incubating unprenylated substrate with a radiolabeled prenyl pyrophosphate precursor in the presence of a soluble yeast cell extract. Radiolabeled protein is detected by a filter-binding assay or by electrophoresing the reaction product on a SDS-polyacrylamide gel.
Chem. 267, 20589 (1992). 12B. He, P. -Y. Chen, K. L. Vancura, S. Michaelis, and S. Powers, Proc. Natl. Acad. Sci. A. 88, 11373 (1991). 13j. F. Moomaw and P. J. Casey, J. Biol. Chem. 267, 17438 (1992). 14y. Reiss, M. C. Seabra, M. S. Brown, and J. L. Goldstein, Biochem. Soc. Trans. 20, 487 (1992). [4] CHARACTERIZATION OF TYPE-n GGTase 23 tion. The assay is performed by incubating unprenylated substrate with a radiolabeled prenyl pyrophosphate precursor in the presence of a soluble yeast cell extract.
Soldati, A. D. Shapiro, J. Lin, and S. R. Pfeffer, J. Cell Biol. 125, 573 (1994). 1 27 as judged by the extent of [ot-32p]GTP binding relative to applied protein. 6 No loss of binding activity has been detected after >2 months of storage at - 2 0 ° in S-100 column buffer containing 40% glycerol. Notes: (1) We have also created a Rab9 protein that possesses a different carboxy-terminal tetrapeptide which serves as a signal for isoprenylation by prenyltransferase I. The resulting Rab9-CLLL is not degraded during the purification process, suggesting that a carboxypeptidase initiates the proteolytic processing and preferentially cleaves Rab9 protein terminating in CC.
Hydrogen bonding in biological structures by George A. Jeffrey
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