化学
离子
化学物理
水溶液
牛血清白蛋白
放松(心理学)
溶菌酶
分子动力学
结晶学
分析化学(期刊)
计算化学
物理化学
色谱法
有机化学
生物化学
社会心理学
心理学
作者
Tadeja Janc,Jean-Pierre Korb,Miha Lukšič,Vojko Vlachy,Robert G. Bryant,Guillaume Mériguet,Natalie Malikova,Anne‐Laure Rollet
标识
DOI:10.1021/acs.jpcb.1c02513
摘要
Proteins function in crowded aqueous environments, interacting with a diverse range of compounds, and among them, dissolved ions. These interactions are water-mediated. In the present study, we combine field-dependent NMR relaxation (NMRD) and theory to probe water dynamics on the surface of proteins in concentrated aqueous solutions of hen egg-white lysozyme (LZM) and bovine serum albumin (BSA). The experiments reveal that the presence of salts (NaCl or NaI) leads to an opposite ion-specific response for the two proteins: an addition of salt to LZM solutions increases water relaxation rates with respect to the salt-free case, while for BSA solutions, a decrease is observed. The magnitude of the change depends on the ion identity. The developed model accounts for the non-Lorentzian shape of the NMRD profiles and reproduces the experimental data over four decades in Larmor frequency (10 kHz to 110 MHz). It is applicable up to high protein concentrations. The model incorporates the observed ion-specific effects via changes in the protein surface roughness, represented by the surface fractal dimension, and the accompanying changes in the surface water residence times. The response is protein-specific, linked to geometrical aspects of the individual protein surfaces, and goes beyond protein-independent Hofmeister-style ordering of ions.
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