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 innovations in protein NMR, less than the organic Magnetic Resonance sequence. quantity sixteen, with the subtitle smooth thoughts in Protein NMR , is the 1st during this sequence. those volumes current a few of the fresh, major advances within the biomolecular NMR box with emphasis on advancements over the last 5 years. we're venerated to have introduced jointly in those quantity a few of the global s ideal specialists who've supplied vast management in advancing this box. quantity sixteen comprises - vances in large different types: I. huge Proteins, Complexes, and Membrane Proteins and II. Pulse tools. quantity 17 comprises significant advances in: I. Com- tational equipment and II. constitution and Dynamics. the hole bankruptcy of quantity 17 begins with a attention of a few vital points of modeling from spectroscopic and diffraction info through Wilfred van Gunsteren and his colleagues. the subsequent chapters care for mixed automatic assignments and protein constitution choice, a space of excessive learn in lots of laboratories because the conventional guide equipment are usually insufficient or arduous in dealing with huge volumes of NMR information on huge proteins. First, Werner Braun and his affiliates describe their adventure with the NOAH/DIAMOD protocol constructed of their laboratory.
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Additional resources for Biological Magnetic Resonance: Structure Computation and Dynamics in Protein NMR
One thus searches observed patterns for characteristic subgraphs representing these connectivities. Figures 1 to 3 show graphic repre- 42 sentations of three types of regular secondary structures: Yuan Xu et al. , 1993; Lau, 1989; Born and Kerbosch, 1973) can be used to search all the secondary structure connectivity patterns in the NOESY spectrum and match them with the NOE templates connectivity patterns and, thus, identify the secondary structure connectivity patterns in the NOESY spectrum. 2.
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Biological Magnetic Resonance: Structure Computation and Dynamics in Protein NMR by Wilfred F. van Gunsteren, Alexandre M. J. J. Bonvin, Xavier Daura, Lorna J. Smith (auth.), N. Rama Krishna, Lawrence J. Berliner (eds.)