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Amino acids, recognition

Archontis, G. Simonson, T. Karplus, M., Binding free energies and free energy components from molecular dynamics and Poisson-Boltzmann calculations. Application to amino acid recognition by aspartyl-tRNA synthetase, J. Mol. Biol. 2001, 306, 307-327... [Pg.460]

Distribution of proteins to tissues is controlled by the permeability (porosity) of the vasculatures and thereby influenced by the molecular size of the protein. A protein of greater than 150kDa ( 50nm) in size will have limited distribution and may be restricted to blood volume. Infrequently a large protein has amino acid recognition sequences that allow passage across epithelial cells lining the vasculatures by transcy-tosis, a process that allows directional transport of protein into and out of a cell. [Pg.105]

GL Challis, J Ravel, CA Townsend. Predictive, structure-based model of amino acid recognition by nonribosomal peptide synthetase adenylation domains. Chem Biol 7 211-224, 2000. [Pg.34]

M. Sawada et al., Chiral amino acid recognition detected by electrospray ionization (ESI) and fast atom bombardment (FAB) mass spectrometry (MS) coupled with the enantiomer-labelled (EL) guest method. J. Chem. Soc. Perkin Trans. 2, 701-710 (1998)... [Pg.83]

Archontis G, Simonson T, Moras D, Karplus M (1998) Specific amino acid recognition by aspartyl-tRNA synthetase studied by free energy simulation, J Mol Biol, 275 823-846... [Pg.338]

Energies and Free Energy Components from Molecular Dynamics and Polsson-Boltzmann Calculations. Application to Amino Acid Recognition by Aspartyl-tRNA Synthetase. [Pg.85]

Most caspase-inhibitor design strategies target their active sites and are based on caspase substrate preferences. Tetrapep-tide inhibitors, which are based on identihed sequences of the four amino acid recognition motifs, were shown to inhibit caspase family members selectively (24) (Fig. 2a). Overall, a typical peptide-based caspase inhibitor consists of three major structural components ... [Pg.171]

L. Serre, G. Verdon, T. Choinowski, N. Hervouet, J.L. Risler, and C. Zelwer. 2001. Ho v methionyl-tRNA synthetase creates its amino acid recognition pocket upon 1-methionine binding J. Mol. Biol. 306 863-876. (PubMed)... [Pg.1246]

P. Schimmel and E. Schmidt Making connections RNA-dependent amino acid recognition. Trends in Biomedical Science 20, 1 (1995). [Pg.591]

Gietzen DW. 2000. Amino acid recognition in the central nervous system. Neural and Metabolic Control of Macro-nutrient Intake, Chapter 23. Berthoud HR, Seeley RJ, editors. New York CRC Press pp. 339-357. (Includes pharmacology of neurotransmitter signaling in the APC down-stream of AA sensing)... [Pg.265]

Serre, L.. Verdon, G.. Choinowski, T., Hervouct, N., Risler, J. L, and Zelwer, C. 2001. How methionyl-tRNA. synthetase creates its amino acid recognition pocket upon l,-methionine binding./. Mol Biol 306 863-876. [Pg.888]

Nicoletti. F., Meek, J.L., ladarola, M.J., Chuang, D.M., Roth, B.L., Costa. E., 1986. Coupling of inositol phospholipid metabolism with excitatory amino acid recognition sites in rat hippocampus. J. Neu-rochem. 46, 40-46. [Pg.168]

Kuroda Y, Kato Y. Chiral amino acid recognition by a porphyrin-based artificial receptor. J Am Chem Soc 1995 117 10950-8. [Pg.464]

Metal ions can bind amino and carboxylate groups (vide supra), so are well-adapted to amino acid recognition. The cobalt(II) complex 33 (racemic) reacts with DL-alanine to give diastereomeric products 34 and 35 in 2 1 ratio. A controlling influence is the tendency of the carboxylates to locate trans to each other. Interestingly, 35 is converted almost exclusively to 34 upon treatment with... [Pg.239]

Fig. 5 Two RET"based sensing schemes. A molecular beacon structure with a fluorescent donor (D) and a quenches (Q) enhances emission upon target hybridization. A protease substrate with donor and acceptor conjugated to an amino acid recognition sequence (DEVD) enhances emission upon enzymatic cleavage. (View this art xi color at www.dekker.com.)... Fig. 5 Two RET"based sensing schemes. A molecular beacon structure with a fluorescent donor (D) and a quenches (Q) enhances emission upon target hybridization. A protease substrate with donor and acceptor conjugated to an amino acid recognition sequence (DEVD) enhances emission upon enzymatic cleavage. (View this art xi color at www.dekker.com.)...
Kuroda. Y. Kato, Y. Higashioji, T. Hasegawa, J. Kawanami, S. Takahashi, M. Shiraishi, N. Tanabe, K. Ogoshi. H. Chiral amino acid recognition by a porphyrin based artificial receptor. J. Am. Chem. Soc. 1995, 117. 10950. [Pg.1148]

Huang, J., Wei, Z., and Chen, J. (2008). Molecular imprinted polypyrrole nanowires for chiral amino acid recognition. Sens. Actuators B. 134, 573-578. [Pg.614]

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See also in sourсe #XX -- [ Pg.339 ]



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