Nuclear Magnetic Resonance of Biomolecules

作者: Jeremy N.S. Evans

DOI: 10.1002/9780470027318.A0210

关键词:

摘要: Nuclear magnetic resonance (NMR) spectroscopy exploits a property of the nucleus known as nuclear spin, which exhibits angular momentum and such generates local field that can be influenced by larger static external field. In presence large magnet, spins align with field, slight excess opposed to That small flipped alignment in radiofrequency (RF) pulse appropriate frequency. Relaxation those back ground state results emission RF radiation whose frequency is an indication electron density molecule spin resides. Such information ultimately directly related molecular structure. NMR unique it used image whole human body at one extreme, determine three-dimensional (3D) structure biomolecule within other extreme. The principal advantages are that: (i) complete determined; (ii) technique spans all states matter (solid, liquid, gas); (iii) method nondestructive noninvasively, clinical setting. disadvantages very insensitive (typically samples below 50 µM difficult study, although recent advances nanoprobe cryprobe technology rapidly revising these numbers); liquids there weight limits around 50 kDa – new methods being developed may have significant impact on this; solids only limited structural obtained date.

参考文章(196)
Frank Löhr, Heinz Rüterjans, A new triple-resonance experiment for the sequential assignment of backbone resonances in proteins. Journal of Biomolecular NMR. ,vol. 6, pp. 189- 197 ,(1995) , 10.1007/BF00211783
Stephan Seip, Jochen Balbach, Horst Kessler, A simple way for sequential assignment in isotopically enriched proteins using a H(N)CACO correlation Journal of Biomolecular NMR. ,vol. 3, pp. 233- 237 ,(1993) , 10.1007/BF00178265
Andy C Wang, Patricia J Lodi, Jun Qin, Geerten W Vuister, Angela M Gronenborn, G Marius Clore, An efficient triple-resonance experiment for proton-directed sequential backbone assignment of medium-sized proteins. Journal of Magnetic Resonance, Series B. ,vol. 105, pp. 196- 198 ,(1994) , 10.1006/JMRB.1994.1123
RasmusH. Fogh, Dick Schipper, Rolf Boelens, Robert Kaptein, 1H, 13C and 15N NMR backbone assignments of the 269-residue serine protease PB92 from Bacillus alcalophilus Journal of Biomolecular NMR. ,vol. 4, pp. 123- 128 ,(1994) , 10.1007/BF00178340
Gareth A. Morris, Ray Freeman, ENHANCEMENT OF NUCLEAR MAGNETIC RESONANCE SIGNALS BY POLARIZATION TRANSFER Journal of the American Chemical Society. ,vol. 101, pp. 760- 762 ,(1979) , 10.1021/JA00497A058
W.E.J.R. Maas, W.S. Veeman, Natural abundance 13C spin diffusion enhanced by magic-angle spinning Chemical Physics Letters. ,vol. 149, pp. 170- 174 ,(1988) , 10.1016/0009-2614(88)87216-6
Susan M. Holl, Garland R. Marshall, Denise D. Beusen, Karol Kociolek, Adam S. Redlinski, Miroslaw T. Leplawy, Robert A. McKay, Shimon Vega, Jacob Schaefer, Determination of an 8-Å interatomic distance in a helical peptide by solid-state NMR spectroscopy Journal of the American Chemical Society. ,vol. 114, pp. 4830- 4833 ,(1992) , 10.1021/JA00038A056
E.R. Andrew, A. Bradbury, R.G. Eades, V.T. Wynn, NUCLEAR CROSS-RELAXATION INDUCED BY SPECIMEN ROTATION Physics Letters. ,vol. 4, pp. 99- 100 ,(1963) , 10.1016/0031-9163(63)90123-9
Yan Li, Florian Krekel, Cecilia A. Ramilo, Nikolaus Amrhein, Jeremy N.S. Evans, Time‐resolved solid‐state REDOR NMR studies of UDP N‐acetylglucosamine enolpyruvyl transferase FEBS Letters. ,vol. 377, pp. 208- 212 ,(1995) , 10.1016/0014-5793(95)01338-5
Clare P. Grey, Astrid P.A.M. Eijkelenboom, Wiebren S. Veeman, 14N Population transfers in two-dimensional 13C14N1H triple-resonance magic-angle spinning nuclear magnetic resonance spectroscopy Solid State Nuclear Magnetic Resonance. ,vol. 4, pp. 113- 120 ,(1995) , 10.1016/0926-2040(94)00041-A