By Frances Separovic (ed.), Akira Naito (ed.)
The complexity and heterogeneity of organic structures has posed an enormous problem lately. An more and more vital instrument for acquiring molecular and atomic scale details on a number huge organic molecules and mobile elements is solid-state NMR. this method can deal with attention-grabbing difficulties in structural biology, together with the association of supramolecular complexes and fibril formation relating to molecular folding, misfolding and aggregation. Advances in organic Solid-State NMR brings the reader brand new with chapters from foreign leaders of this starting to be box, masking the latest advancements within the technique and functions of solid-state NMR to reviews of membrane interactions and molecular motions. a far wanted dialogue of membrane structures is certain along very important advancements in in situ research. themes contain purposes to organic membranes, membrane lively peptides, membrane proteins, protein assemblies and in-cell NMR. This exposition of a useful strategy will curiosity these operating in various comparable spectroscopic and organic fields. A easy advent invitations these to familiarise themselves with the fundamental mathematical and conceptual foundations of solid-state NMR. an intensive and accomplished dialogue of this promising approach follows, with a view to be crucial interpreting for these operating or learning at postgraduate point during this interesting box.
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Additional info for Advances in Biological Solid-State NMR: Proteins and Membrane-Active Peptides
Brooks III, A. D. MacKerell Jr, L. Nilsson, R. J. Petrella, B. Roux, Y. Won, G. Archontis, C. Bartels, S. Boresch, A. Caflisch, L. Caves, Q. Cui, A. R. Dinner, M. Feig, S. Fischer, J. Gao, M. Hodoscek, W. Im, K. Kuczera, T. Lazaridis, J. Ma, V. Ovchinnikov, E. Paci, R. W. Pastor, C. B. Post, J. Z. Pu, M. Schaefer, B. Tidor, R. M. Venable, H. L. Woodcock, X. Wu, W. Yang, D. M. York and M. Karplus, J. Comput. , 2009, 30, 1545. 31. R. Bertram, T. Asbury, F. Fabiola, J. R. Quine, T. A. Cross and M.
D) 3D plot demonstrating the relationship between plots (A–C). The tilt, t, determines the amplitude of the dipolar or CS waves and size of the PISA wheel, while the rotation, r, determines the phase of the waves. Intertwined wheels are observed in (C). Waves were generated using average Da and principal elements for the 15N chemical shift tensor interaction. peptide in the bilayer. The use of dipolar waves and MD simulations to assist in the assignment of DC signals from multiply labeled peptides is also presented.
2011, 7, 263–270. 48. K. Seidel, A. Lange, S. Becker, C. E. Hughes, H. Heise and M. Baldus, Phys. Chem. Chem. , 2004, 6, 5090–5093. 49. M. Weingarth, G. Bodenhausen and P. Tekely, J. Am. Chem. , 2009, 131, 13937–13939. 50. T. Gullion and J. Schaefer, J. Magn. , 1989, 81, 196–200. CHAPTER 2 Combining NMR Spectroscopic Measurements and Molecular Dynamics Simulations to Determine the Orientation of Amphipathic Peptides in Lipid Bilayers B. ,a RICHARD W. 1–12 At minimum, they corroborate measured and theoretical properties.
Advances in Biological Solid-State NMR: Proteins and Membrane-Active Peptides by Frances Separovic (ed.), Akira Naito (ed.)