By Frances Separovic (ed.), Akira Naito (ed.)
The complexity and heterogeneity of organic platforms has posed an important problem in recent times. An more and more vital software for acquiring molecular and atomic scale details on more than a few huge organic molecules and mobile elements is solid-state NMR. this system can tackle interesting difficulties in structural biology, together with the association of supramolecular complexes and fibril formation on the subject of molecular folding, misfolding and aggregation. Advances in organic Solid-State NMR brings the reader modern with chapters from foreign leaders of this transforming into box, protecting the latest advancements within the method and purposes of solid-state NMR to reviews of membrane interactions and molecular motions. a miles wanted dialogue of membrane structures is exact along very important advancements in in situ research. issues contain purposes to organic membranes, membrane lively peptides, membrane proteins, protein assemblies and in-cell NMR. This exposition of a useful method will curiosity these operating in a variety of comparable spectroscopic and organic fields. A easy creation invitations these to familiarise themselves with the elemental mathematical and conceptual foundations of solid-state NMR. an intensive and complete dialogue of this promising method follows, as a way to be crucial analyzing for these operating or learning at postgraduate point during this intriguing box.
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Additional resources for Advances in Biological Solid-State NMR: Proteins and Membrane-Active Peptides
Ernst, A. Samoson and B. H. Meier, J. Magn. , 2003, 163, 332–339; (c) M. Weingarth, G. Bodenhausen and P. Tekely, J. Magn. , 2009, 199, 238–241. 21. M. Lee and W. I. Goldburg, Phys. , 1965, 140, 1261–1271. 22. (a) A. Bielecki, A. C. Kolbert and M. H. Levitt, Chem. Phys. , 1989, 155, 341–346; (b) E. Vinogradov, P. K. Madhu and S. Vega, Chem. Phys. , 1999, 314, 443–450. 23. (a) M. E. Halse and L. Emsley, Phys. Chem. Chem. , 2012, 14, 9121–9130; (b) P. K. Madhu, Solid State Nucl. Magn. , 2009, 35, 2–11.
30–32,49 Left, bottom: A two-dimensional NCA spectrum of a protein sample. Right: Spin diﬀusion magnetization transfer requires spectral overlap, which can be achieved by switching oﬀ the 1H decoupling during the mixing time. At higher MAS frequencies, heteronuclear dipolar couplings are significantly reduced by MAS, which curtails the spin diﬀusion eﬃciency. With active recoupling, here shown by the example of PARIS31 recoupling, the spectral broadening is independent of the MAS frequency (signals are normalized).
M. Weingarth, C. Ader, A. J. S. Melquiond, D. Nand, O. Pongs, S. Becker, A. Bonvin and M. Baldus, Biophys. , 2012, 103, 29. 12. S. Jo and W. Im, Biophys. , 2011, 100, 2913. 13. C. H. Wu, A. Ramamoorthy and S. J. Opella, J. Magn. , Ser. A, 1994, 109, 270. 14. R. Fu and T. A. Cross, Annu. Rev. Biophys. Biomol. , 1999, 28, 235. 15. S. J. Opella and F. M. Marassi, Chem. , 2004, 104, 3587. 16. F. M. Marassi, B. B. Das, G. J. Lu, H. J. Nothnagel, S. H. Park, W. S. Son, Y. Tian and S. J. Opella, Methods, 2011, 55, 363.
Advances in Biological Solid-State NMR: Proteins and Membrane-Active Peptides by Frances Separovic (ed.), Akira Naito (ed.)