Multidimensional cross-correlation relaxometry of aqueous protein systems

被引：24
|
作者：
Venturi, L. [1 ]
Woodward, N. [1 ]
Hibberd, D. [1 ]
Marigheto, N. [1 ]
Gravelle, A. [1 ]
Ferrante, G. [1 ]
Hills, B. P. [1 ]
机构：
[1] Inst Food Res, Norwich NR4 7UA, Norfolk, England
来源：
APPLIED MAGNETIC RESONANCE | 2008年 / 33卷 / 03期
关键词：
D O I：
10.1007/s00723-008-0066-z
中图分类号：
O64 [物理化学（理论化学）、化学物理学]; O56 [分子物理学、原子物理学];
学科分类号：
070203 ; 070304 ; 081704 ; 1406 ;
摘要：
We report, for the first time, the application of multidimensional cross-correlation relaxometry to a model globular aqueous protein system (bovine serum albumin) over a wide range of water contents from the solution to glassy states. Off-diagonal cross-relaxation peaks are observed and lend support to the proton-exchange cross-relaxation model of water relaxation. The dependence of the water proton relaxation rates on water content is also consistent with the multistate theory of water dynamics in protein systems. Evidence for water compartmentation in bovine serum albumin gels is presented and the potential of multidimensional cross-correlation nuclear magnetic resonance relaxometry in elucidating water-biopolymer interactions in more complex heterogeneous biopolymer systems is discussed.
引用
收藏
页码：213 / 234
页数：22
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