硒代半胱氨酸
分子动力学
半胱氨酸
化学
力场(虚构)
质子化
背景(考古学)
从头算
计算化学
氨基酸
分子力学
硫醇
生物化学
物理
有机化学
生物
酶
古生物学
离子
量子力学
作者
Federico N. Pedron,Andresa Messias,Ari Zeida,Adrián E. Roitberg,Darío A. Estrı́n
标识
DOI:10.1021/acs.jcim.2c01104
摘要
Cysteine is a common amino acid with a thiol group that plays a pivotal role in a variety of scenarios in redox biochemistry. In contrast, selenocysteine, the 21st amino acid, is only present in 25 human proteins. Classical force-field parameters for cysteine and selenocysteine are still scarce. In this context, we present a methodology to obtain Lennard-Jones parameters for cysteine and selenocysteine in different physiologically relevant oxidation and protonation states. The new force field parameters obtained in this work are available at https://github.com/MALBECC/AMBER-parameters-database. The parameters were adjusted to reproduce water radial distribution functions obtained by density functional theory ab initio molecular dynamics. We validated the results by evaluating the impact of the choice of parameters on the structure and dynamics in classical molecular dynamics simulations of representative proteins containing catalytic cysteine/selenocysteine residues. There are significant changes in protein structure and dynamics depending on the parameters choice, specifically affecting the residues close to the catalytic sites.
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