Specific protein-urea interactions

作     者：Zhi Wei Wong Daiwen Yang Zhi Wei Wong;Daiwen Yang

作者机构：Department of Biological SciencesNational University of Singapore14 Science Drive 4Singapore117543Singapore 

出 版 物：《Magnetic Resonance Letters》 (磁共振快报（英文）)

年 卷 期：2022年第2卷第3期

页      面：131-138页

核心收录：

学科分类：081704[工学-应用化学] 07[理学] 08[工学] 0817[工学-化学工程与技术] 070303[理学-有机化学] 0703[理学-化学] 

基　　金：supported by a grant to D.Y.from Singapore Ministry of Education Academic Research Fund Tier 1(R154-000-C03e114 or A-0004464-00-00) 

主　　题：Protein denaturation Protein-folding Fatty acid binding protein Hydrogen-deuterium exchange 

摘      要：The mechanism of urea s action in protein denaturation remains largely *** provide an experimental basis for molecular dynamics(MD)simulations on urea-protein interactions,we investigated the effect of urea on human intestinal fatty acid binding protein(hIFABP)by nuclear magnetic resonance(NMR).Hydrogen-deuterium exchange(HDX)rates at
2 M urea indicate that urea affects hIFABP in a residue-specific manner via direct urea-protein interactions and preferentially weakens hydrogen bonds between highly protected ***-specific effects of urea on NMR peak intensities and chemical shifts further support the presence of direct urea-protein ***(2D)water-rotating frame Overhauser enhancement(ROE)data shows one protein-bound water molecule in contact with Val66 and Trp82,one putative bound water molecule in interaction with Thr76 and E-F loop,and that urea at low concentrations cannot displace these protein-bound water *** urea-nuclear Overhauser effect(NOE)experiments using 15N-urea further show no tightly protein-bound urea *** results thus suggest specific,but weak or transient,urea-protein interactions,supporting the direct interaction model of urea denaturation.