当前位置: X-MOL 学术J. Am. Chem. Soc. › 论文详情
Slow Dynamics of Tryptophan–Water Networks in Proteins
Journal of the American Chemical Society ( IF 14.357 ) Pub Date : 2018-01-03 , DOI: 10.1021/jacs.7b09974
R. Bryn Fenwick, David Oyen, H. Jane Dyson, Peter E. Wright

Water has a profound effect on the dynamics of biomolecules and governs many biological processes, leading to the concept that function is slaved to solvent dynamics within and surrounding the biomolecule. Protein conformational changes on μs–ms time scales are frequently associated with protein function, but little is known about the behavior of protein-bound water on these time scales. Here we have used NMR relaxation dispersion measurements to probe the tryptophan indoles in the enzyme dihydrofolate reductase (DHFR). We find that during structural changes on the μs–ms time scale, large chemical shift changes are often observed for the NH proton on the indole ring, while relatively smaller chemical shift changes are observed for the ring nitrogen atom. Comparison with experimental chemical shifts and density functional theory-based chemical shift predictions show that during the structural change the tryptophan indole NHs remain bound to water, but the geometry of the protein-bound water networks changes. These results establish that relaxation dispersion measurements can indirectly probe water dynamics and indicate that water can influence, or be influenced by, protein conformational changes on the μs–ms time scale. Our data show that structurally conserved bound water molecules can play a critical role in transmitting information between functionally important regions of the protein and provide evidence that internal protein motions can be coupled through the mediation of hydrogen-bonded water bound in the protein structure.
更新日期:2018-01-03

 

分享到
评论: 0
期刊列表
投票
nature
Nature
Nature
哈尔滨工业大学刘绍琴教授课题组诚招博士后、科研助理
新加坡国立大学-深圳大学联合招聘STM博士后
南方科技大学化学系黄乃正院士团队招聘
陆军军医大学组织器官再生工程研究中心招聘研究员及科研助理
【问答】请问木质素与环氧氯丙烷是否发生反应,反应产物是什么?
天合科研
2017年中科院JCR分区化学大类列表
试剂库存管理
化合物查询
down
wechat
bug