Molecular dynamics analysis of the conformations of a beta-hairpin miniprotein.
Molecular dynamics analysis of the conformations of a beta-hairpin miniprotein.
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DOI：
10.1021/jp910465e
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发表时间：
2010-03-04
期刊：
影响因子：
--
通讯作者：
Lovas S
中科院分区：
文献类型：
--
作者：
Hatfield MP;Murphy RF;Lovas S
采用分子动力学方法模拟了一种β-发夹微蛋白CLN 025在278 K、300 K、333 K和363 K的水溶液中以及在300 K的TFE、MeOH和DMSO溶液中的构象稳定性. CLN 025是Chignolin微蛋白的变体，其中Chignolin的末端Gly残基被Tyr残基取代，这导致解链温度增加29.7 K。在BH和HLYP/cc-pVTZ理论水平上使用DFT量子化学计算计算分子内相互作用的能量。CLN 025在所有环境中保持β-发夹构象。β-发夹通过氢键、肽的带电末端之间的静电相互作用和弱极性相互作用来稳定。N端和C端主链之间的相互作用占稳定能的−97.32至−120.87 kcal mol−1。Tyr 2和Pro 4之间的CH-π相互作用的能量在−1.80和−8.9 kcal mol−1之间，Tyr 2-Trp 9 Ar-Ar相互作用的能量在−0.43和−8.11 kcal mol−1之间。温度升高导致Tyr 2-Pro4 CH-π以及Tyr 2-Trp 9和Tyr 2-Tyr 10 Ar-Ar相互作用变得不那么有利，但Tyr 1-Trp 9相互作用变得更加有利，并在稳定CLN 025的β-发夹中发挥重要作用，导致熔解温度升高。弱极性相互作用对CLN 025和其他蛋白质的结构和稳定性起着重要作用。
Molecular Dynamics simulations of a β-hairpin miniprotein, CLN025, were performed to examine the conformational stability of the peptide in H2O at 278 K, 300 K, 333 K and 363 K as well as in TFE, MeOH and DMSO at 300 K. CLN025 is a variant of the Chignolin miniprotein, in which the terminal Gly residues of Chignolin are replaced with Tyr residues, which leads to a 29.7 K increase in melting temperature. The energy of the intramolecular interactions were calculated using DFT quantum chemical calculations at the BH and HLYP/cc-pVTZ level of theory. CLN025 maintained a β-hairpin conformation in all environments. The β-hairpin is stabilized by hydrogen bonds, an electrostatic interaction between the charged termini of the peptide and weakly polar interactions. The interaction between the backbones of the N and C-terminal strands accounts for −97.32 to −120.87 kcal mol−1 of the stabilization energy. The energy of the CH-π interactions between Tyr2 and Pro4 were between −1.80 and −8.9 kcal mol−1 and the energy of the Tyr2-Trp9 Ar-Ar interaction was between −0.43 and −8.11 kcal mol−1. Increasing temperature caused the Tyr2-Pro4 CH-π and the Tyr2-Trp9 and Tyr2-Tyr10 Ar-Ar interactions to become less favorable but the Tyr1-Trp9 interaction became more favorable and played an important role in stabilizing the β-hairpin of CLN025 that resulted in the increased melting temperature. The weakly polar interactions play an important role in the structure and stability of CLN025 and other proteins.
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