Biological Magnetic Resonance: Structure Computation and by Wilfred F. van Gunsteren, Alexandre M. J. J. Bonvin, Xavier

By Wilfred F. van Gunsteren, Alexandre M. J. J. Bonvin, Xavier Daura, Lorna J. Smith (auth.), N. Rama Krishna, Lawrence J. Berliner (eds.)

Volume 17 is the second one in a distinct subject sequence dedicated to sleek ideas in protein NMR, less than the organic Magnetic Resonance sequence. quantity sixteen, with the subtitle smooth strategies in Protein NMR , is the 1st during this sequence. those volumes current many of the contemporary, major advances within the biomolecular NMR box with emphasis on advancements over the past 5 years. we're venerated to have introduced jointly in those quantity the various international s best specialists who've supplied extensive management in advancing this box. quantity sixteen comprises - vances in extensive different types: I. huge Proteins, Complexes, and Membrane Proteins and II. Pulse tools. quantity 17 includes significant advances in: I. Com- tational tools and II. constitution and Dynamics. the outlet bankruptcy of quantity 17 starts off with a attention of a few very important elements of modeling from spectroscopic and diffraction facts through Wilfred van Gunsteren and his colleagues. the following chapters care for mixed automatic assignments and protein constitution selection, a space of severe learn in lots of laboratories because the conventional guide tools are usually insufficient or exhausting in dealing with huge volumes of NMR facts on huge proteins. First, Werner Braun and his affiliates describe their event with the NOAH/DIAMOD protocol constructed of their laboratory.

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A225, Plenum, New York, pp. 209–217. Schiffer, C. , and van Gunsteren, W. , 1995, Acta Crystallogr. Sect. D 51:85. Schiffer, C. , and van Gunsteren, W. , 1994, J. Mot Biol. 241:588. , and James, T. , 1992, J. Am. Chem. Soc. 114:10654. Smith, L. , Mark, A. , Dobson, C. , and van Gunsteren, W. , 1995, Biochemistry 34:10918. Stein, E. , Rice, L. , and Brünger, A. , 1997, J. Magn. Reson. 124:154. Torda, A. , Brunne, R. , and van Gunsteren, W. , 1993, J. Biomol. NMR 3:55. Torda, A. , Scheek, R. , and van Gunsteren, W.

1958, J. Chem. Phys. 29:1012. , Zuiderweg, E. R. , Scheek, R. , and van Gunsteren, W. , 1985, J. Mol. Biol. 182:179. , 1959, J. Chem. Phys. 30:11. , 1963, J. Am. Chem. Soc. 85:2870. , and Somorjay, R. , 1979, Comp. Chem. 3:25. , Gronenborn, A. , and Clore, G. , 1995a, J. Magn. Reson. B107:293. , Gronenborn, A. , and Clore, G. , 1995b, J. Magn. Reson. B106:92. Luty, B. , Davis, M. , Tironi, I. , and van Gunsteren, W. , 1994, Mol. Simulation 14:11. , and Friedman, A. , 1990, Biophys. J. 58:803.

Reliable and accurate methods of assigning cross peaks in experimental NOESY spectra will be needed to handle the increased number of 3D structure determinations and to allow analysis of larger proteins. Computer analysis of spectra, despite its lack of the (human) “innate massively parallel visual” processor (Nigles, 1996), becomes even more desirable for multidimensional spectra with labeled proteins (Zimmerman and Montelione, 1995; Oschkinat and Croft, 1994). The emphasis in this chapter will be on concepts and computational methods rather than on specific programs.

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