An effective method for the discrimination of motional anisotropy and chemical exchange

被引:143
作者
Kneller, JM [1 ]
Lu, M [1 ]
Bracken, C [1 ]
机构
[1] Cornell Univ, Weill Med Coll, Dept Biochem, New York, NY 10021 USA
关键词
D O I
10.1021/ja017461k
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
Analysis of the ratio of transverse and longitudinal relaxation rates (R2/R1) is an approach commonly used for estimation of overall correlation time and identification of chemical exchange in biological macromolecules. However, this analysis fails to distinguish between chemical exchange and motional anisotropy. We describe a simple method for identifying chemical exchange and motional anisotropy using the product, R1R2. In the slow tumbling regime, the R1R2 product results in a constant value that is independent of overall correlation time and motional anisotropy. This analysis provides a simple method for rapidly estimating and dissociating the effects of motional anisotropy and chemical exchange in NMR heteronuclear spin relaxation data. We demonstrate the utility of the method with 15N relaxation data collected on the proteins E. coli ribonuclease H and the trimeric E. coli membrane associated lipoprotein lpp. Copyright © 2002 American Chemical Society.
引用
收藏
页码:1852 / 1853
页数:2
相关论文
共 18 条
[1]   Monitoring macromolecular motions on microsecond to millisecond time scales by R(1)rho-R(1) constant relaxation time NMR spectroscopy [J].
Akke, M ;
Palmer, AG .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1996, 118 (04) :911-912
[2]   Temperature dependence of intramolecular dynamics of the basic leucine zipper of GCN4: Implications for the entropy of association with DNA [J].
Bracken, C ;
Carr, PA ;
Cavanagh, J ;
Palmer, AG .
JOURNAL OF MOLECULAR BIOLOGY, 1999, 285 (05) :2133-2146
[3]   The use of residual dipolar coupling in concert with backbone relaxation rates to identify conformational exchange by NMR [J].
de Alba, E ;
Baber, JL ;
Tjandra, N .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1999, 121 (17) :4282-4283
[4]   HYDRONMR: Prediction of NMR relaxation of globular proteins from atomic-level structures and hydrodynamic calculations [J].
de la Torre, JG ;
Huertas, ML ;
Carrasco, B .
JOURNAL OF MAGNETIC RESONANCE, 2000, 147 (01) :138-146
[5]   Protein dynamics from NMR [J].
Kay, LE .
NATURE STRUCTURAL BIOLOGY, 1998, 5 (Suppl 7) :513-517
[6]   BACKBONE DYNAMICS OF PROTEINS AS STUDIED BY N-15 INVERSE DETECTED HETERONUCLEAR NMR-SPECTROSCOPY - APPLICATION TO STAPHYLOCOCCAL NUCLEASE [J].
KAY, LE ;
TORCHIA, DA ;
BAX, A .
BIOCHEMISTRY, 1989, 28 (23) :8972-8979
[7]   Variability of the 15N chemical shift anisotropy in Escherichia coli ribonuclease H in solution [J].
Kroenke, CD ;
Rance, M ;
Palmer, AG .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1999, 121 (43) :10119-10125
[8]   Longitudinal and transverse 1H-15N dipolar 15N chemical shift anisotropy relaxation interference:: Unambiguous determination of rotational diffusion tensors and chemical exchange effects in biological macromolecules [J].
Kroenke, CD ;
Loria, JP ;
Lee, LK ;
Rance, M ;
Palmer, AG .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1998, 120 (31) :7905-7915
[9]   Rotational diffusion anisotropy of proteins from simultaneous analysis of N-15 and C-13(alpha) nuclear spin relaxation [J].
Lee, LK ;
Rance, M ;
Chazin, WJ ;
Palmer, AG .
JOURNAL OF BIOMOLECULAR NMR, 1997, 9 (03) :287-298
[10]   MODEL-FREE APPROACH TO THE INTERPRETATION OF NUCLEAR MAGNETIC-RESONANCE RELAXATION IN MACROMOLECULES .1. THEORY AND RANGE OF VALIDITY [J].
LIPARI, G ;
SZABO, A .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1982, 104 (17) :4546-4559