Understanding folding and design: Replica-exchange simulations of "Trp-cage" fly miniproteins
Understanding folding and design: Replica-exchange simulations of "Trp-cage" fly miniproteins
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DOI：
10.1073/pnas.1330954100
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发表时间：
2003-06-24
影响因子：
11.1
通讯作者：
Swope, W
中科院分区：
文献类型：
--
作者：
Pitera, JW;Swope, W
采用复制交换分子动力学方法，在隐式溶剂中模拟了一个20个氨基酸残基的多肽（或称“小蛋白”）的折叠热力学。“本研究中的模拟使用AMBER（parm 94）力场沿着广义Born/溶剂可及表面积隐式溶剂模型，温度范围为273至630 K。从一个完全扩展的初始构象开始，模拟一个肽序列样本构象，
Replica-exchange molecular dynamics simulations in implicit solvent have been carried out to study the folding thermodynamics of a designed 20-residue peptide, or "miniprotein." The simulations in this study used the AMBER (parm94) force field along with the generalized Born/solvent-accessible surface area implicit solvent model, and they spanned a range of temperatures from 273 to 630 K. Starting from a completely extended initial conformation, simulations of one peptide sequence sample conformations that are