Paramagnetic relaxation enhancement
From NMR Wiki
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url={http://dx.doi.org/10.1021/bi000060h} | url={http://dx.doi.org/10.1021/bi000060h} | ||
} | } | ||
| + | #Shortel bibtex=@article{gillespie1997clr, | ||
| + | title={{Characterization of long-range structure in the denatured state of staphylococcal nuclease. II. distance restraints from paramagnetic relaxation and calculation of an ensemble of structures}}, | ||
| + | author={Gillespie, J.R. and Shortle, D.}, | ||
| + | journal={Journal of Molecular Biology}, | ||
| + | volume={268}, | ||
| + | number={1}, | ||
| + | pages={170--184}, | ||
| + | year={1997}, | ||
| + | url={http://dx.doi.org/10.1006/jmbi.1997.0953} | ||
| + | } | ||
| + | |||
</biblio> | </biblio> | ||
Revision as of 20:41, 7 August 2008
Paramagnetic Relaxation Enhancement(PRE) is increasingly becoming a method to provide long-range distance information that can complement NOE restraints, which are limited to distances of less than 6A. This method can be used to get distances in the range of 15-24A.
- Liang, B and Bushweller, JH and Tamm, LK. Site-directed parallel spin-labeling and paramagnetic relaxation enhancement in structure determination of membrane proteins by solution NMR spectroscopy. J Am Chem Soc 128(13):4389--4397, 2006. BibTeX
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Battiste, JL and Wagner, G. Utilization of site-directed spin labeling and high-resolution heteronuclear nuclear magnetic resonance for global fold determination of large proteins with limited nuclear overhauser effect data. Biochemistry 39(18):5355--65, 2000. BibTeX
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Gillespie, JR and Shortle, D. Characterization of long-range structure in the denatured state of staphylococcal nuclease. II. distance restraints from paramagnetic relaxation and calculation of an ensemble of structures. Journal of Molecular Biology 268(1):170--184, 1997. BibTeX
