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Group biochemistry

Manz, B Stilbs, P Jonsson, B Soderman, O Callaghan, PT, NMR Imaging of the Time Evolution of Electroosmotic Flow in a Capillary, Journal of Physical Chemistry 99, 11297, 1995. Matthew, JB Hanania, GIH Gurd, FRN, Electrostatic Effects in Hemoglobin Bohr Effect and Ionic Strength Dependence of Individual Groups, Biochemistry 18, 1928, 1979. [Pg.616]

Lee, C.-H. Skibo, E. B. Active site directed reductive alkylation of xanthine oxidase by imidazo[4,5-g]quinazoline-4,9-diones functionalized with a leaving group. Biochemistry 1987, 26, 7355-7362. [Pg.264]

Reactions of cy anate with functional groups of proteins. III. Reactions with amino and carboxyl groups. Biochemistry 4, 1030—1036 (1965). [Pg.39]

R. L. Taylor and H. E. Conrad, Stoichiometric depolymerization of polyuronides and glycosaminoglycuronans to monosaccharides following reduction of their carbodiimide-actived carboxyl groups, Biochemistry, 11 (1972) 1383-1388. [Pg.291]

Mattioli, T. A., Williams, J. C., Allen, J. P, and Robert, B., 1994, Changes in primary donor hydrogen-bonding interactions in mutant reaction centers from Rhodobacter sphaeroides Identification of the vibrational frequencies of all the conjugated carbonyl groups. Biochemistry, 33 1636nl643. [Pg.671]

Bowers, K.E., and Fierke, C. A. (2004). Positively charged side chains in protein farnesyltransferase enhance catalysis by stabilizing the formation of the diphosphate leaving group. Biochemistry 43 5256-5265. [Pg.10]

Micah, E., Chehade, K.A.H., Isaacs, R.J., Andres, D.A., and Spielmann, H.P. (2001). Protein farnesyltransferase isoprenoid substrate discrimination is dependent on isoprene double bonds and branched methyl groups. Biochemistry 40 12254-12265. [Pg.125]

Kawai G, Yamamoto Y, Kanrimura T, Masegi T, Sekine M, Hata T, et al. Conformational rigidity of specific pyrimidine residues in tRNA arises from posttranscriptional modifications that enhance steric interaction between the base and the 2 -hydroxyl group. Biochemistry 1992 31 1040-1046. [Pg.1105]

Roberts, M. F., Bothner-By, A. A., and Dennis, E. A. (1978). Magnetic nonequivalence within the fatty acyl chains of phospholipids in membrane models H nuclear magnetic resonance studies of the a-methylene groups. Biochemistry 17,935—942. [Pg.85]

Drummond J, Matthews R 1994 Nitrous oxide inactivation of cobalamin-dependent methionine synthase from Escherichia coli characterization of the damage to the enzyme and prosthetic group. Biochemistry 33 3742-3750... [Pg.303]

Liu, H.H. Walsh, C.T. The Chemistry of the Cyclopropyl Group Biochemistry of Cyclopropyl Group-, Rappoport, Z. Ed. Interscience London, 1987, Chapter 16, p959. [Pg.1057]

L3. Little, J. R., and Eisen, H. N., Physical and chemical differences between rabbit antibodies to the 2,4-dinitrophenol and the 2,4,6-trinitrophenol groups. Biochemistry 7, 711-720 (1968). [Pg.57]

Heering HA, Bulsink YBM, Hagen WR, Meyer TE (1995) Influence of charge and polarity on the redox potentials of high-potential iron-sulfur proteins - evidence for the existence of 2 groups. Biochemistry 34 14675-14686... [Pg.151]

Shukla, R Jelinsky, S., Liu, T., Geactinov, N.E., and Loechler, E.L. (1997) How stereochemistry affects mutagenesis by N2-deoxyguanosine adducts of 7,8-dihydroxy-9,10-epoxy-7,8,9,10-tetrahydrobenzoJaJpyrene configuration of the adduct bond is more important than those of hydroxyl groups. Biochemistry, 36,13263-132639. [Pg.151]

S. Clejan, R. Bittman, P. W. Deroo, Y. A. Isaacson, and A. F. Rosenthal, Permability Properties of Sterol-Containing Liposomes from Analogues of Phosphatidylcholine Lacking Acyl Groups, Biochemistry 18, 2118-2125 (1979). [Pg.477]

Biological Sciences Group, Biochemistry and Biophysics Section, University of Connecticut Storrs, Connecticut 06268, U.S.A. [Pg.73]

Noguchi, T., Fukami, Y., Oh-Oka, H., Inoue, Y. FouiiCT transform infrared study on the primary donor P798 of Heliobacterium modesticaldum Cysteine S-H coupled to P798 and molecular interactions of carbonyl groups. Biochemistry 36, 12329-12336 (1997)... [Pg.321]

Tsong, T.Y. (1976) Ferricytochrome c chain folding measured by the energy transfer of tryptophan 59 to the heme group. Biochemistry, 15, 5467-5473. [Pg.548]


See other pages where Group biochemistry is mentioned: [Pg.1055]    [Pg.243]    [Pg.701]    [Pg.3]    [Pg.266]    [Pg.279]    [Pg.347]    [Pg.681]   
See also in sourсe #XX -- [ Pg.220 ]




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