A PFG NMR experiment for translational diffusion measurements in low-viscosity solvents containing multiple resonances

被引:9
作者
Simorellis, AK [1 ]
Flynn, PF [1 ]
机构
[1] Univ Utah, Dept Chem, Salt Lake City, UT 84112 USA
关键词
PFG diffusion; protein encapsulation; membrane protein; micelle; inverted micelle; reverse micelle; low-viscosity solvents;
D O I
10.1016/j.jmr.2004.07.010
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Pulsed gradient simulated-echo (PGSE) NMR diffusion measurements provide a facile and accurate means for determining the self-diffusion coefficients for molecules over a wide range of sizes and conditions. The measurement of diffusion in solvents of low intrinsic viscosity is particularly challenging, due to the persistent presence of convection. Although convection can occur in most solvent systems at elevated temperatures, in lower viscosity solvents (e.g., short chain alkanes), convection may manifest itself even at ambient laboratory temperatures. In most circumstances, solvent suppression will also be required, and for solvents that have multiple resonances, effective suppression can likewise represent a substantial challenge. In this article, we report an NMR experiment that combines a double-stimulated echo PFG approach with a WET-based solvent suppression scheme that effectively and simultaneously address the issues of dynamic range and the deleterious effects of convection. The experiment described will be of general benefit to studies aimed at the characterization of diffusion of single molecules directly dissolved in low-viscosity solvents, and should also be of substantial utility in studies of supramolecular assemblies such as reverse-micelles dissolved in apolar solvents. (C) 2004 Elsevier Inc. All rights reserved.
引用
收藏
页码:322 / 328
页数:7
相关论文
共 28 条
[1]   ASSOCIATION OF BIOMOLECULAR SYSTEMS VIA PULSED-FIELD GRADIENT NMR SELF-DIFFUSION MEASUREMENTS [J].
ALTIERI, AS ;
HINTON, DP ;
BYRD, RA .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1995, 117 (28) :7566-7567
[2]   Validation of protein structure from preparations of encapsulated proteins dissolved in low viscosity fluids [J].
Babu, CR ;
Flynn, PF ;
Wand, AJ .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2001, 123 (11) :2691-2692
[3]   Preparation, characterization, and NMR spectroscopy of encapsulated proteins dissolved in low viscosity fluids [J].
Babu, CR ;
Flynn, PF ;
Wand, AJ .
JOURNAL OF BIOMOLECULAR NMR, 2003, 25 (04) :313-323
[4]  
Clore GM, 1997, NAT STRUCT BIOL, V4, P849
[5]   Preparation of encapsulated proteins dissolved in low viscosity fluids [J].
Ehrhardt, MR ;
Flynn, PF ;
Wand, AJ .
JOURNAL OF BIOMOLECULAR NMR, 1999, 14 (01) :75-78
[6]   A simple and effective NMR cell for studies of encapsulated proteins dissolved in low viscosity solvents [J].
Flynn, PF ;
Milton, MJ ;
Babu, CR ;
Wand, AJ .
JOURNAL OF BIOMOLECULAR NMR, 2002, 23 (04) :311-316
[7]   High-resolution nuclear magnetic resonance of encapsulated proteins dissolved in low viscosity fluids [J].
Flynn, PF ;
Wand, AJ .
NUCLEAR MAGNETIC RESONANCE OF BIOLOGICAL MACROMOLECULES, PT B, 2001, 339 :54-70
[8]   Optimal use of cryogenic probe technology in NMR studies of proteins [J].
Flynn, PF ;
Mattiello, DL ;
Hill, HDW ;
Wand, AJ .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2000, 122 (19) :4823-4824
[9]   NMR of biomolecules in low viscosity, liquid CO2 [J].
Gaemers, S ;
Elsevier, CJ ;
Bax, A .
CHEMICAL PHYSICS LETTERS, 1999, 301 (1-2) :138-144
[10]   A PFG NMR EXPERIMENT FOR ACCURATE DIFFUSION AND FLOW STUDIES IN THE PRESENCE OF EDDY CURRENTS [J].
GIBBS, SJ ;
JOHNSON, CS .
JOURNAL OF MAGNETIC RESONANCE, 1991, 93 (02) :395-402