Importance of Hydrophilic Hydration and Intramolecular Interactions in the Thermodynamics of Helix-Coil Transition and Helix-Helix Assembly in a Deca-Alanine Peptide.
Importance of Hydrophilic Hydration and Intramolecular Interactions in the Thermodynamics of Helix-Coil Transition and Helix-Helix Assembly in a Deca-Alanine Peptide.
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亲水水合和分子内相互作用在十丙氨酸肽螺旋-螺旋转变和螺旋-螺旋组装的热力学中的重要性。
DOI：
10.1021/acs.jpcb.5b09881
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发表时间：
2016
期刊：
影响因子：
--
通讯作者：
Asthagiri,D
中科院分区：
文献类型：
--
作者：
Tomar,DheerajS;Weber,Valéry;Pettitt,BMontgomery;Asthagiri,D
对于模型十丙氨酸肽的腔（理想的疏水性）的贡献，有利于水化的螺旋状态超过扩展状态和配对的螺旋束在两个螺旋的组装。有吸引力的蛋白质-溶剂相互作用的能量贡献被分离成准化学成分，由第一水合壳层中与溶剂相互作用产生的短程部分和由高斯描述的其余长程部分组成。在螺旋-卷曲转变中，短程有吸引力的蛋白质-溶剂相互作用超过疏水水合作用，并有利于延伸的卷曲状态。对折叠效应的分析表明，肽骨架的有利水合作用有利于未折叠状态。蛋白质分子内的相互作用有利于螺旋状态，并在有利于折叠的决定性。在配对的两个螺旋，空腔的贡献超过了短程吸引力的蛋白质-水的相互作用。然而，长距离的蛋白质-溶剂吸引相互作用可以增强或逆转这种趋势，这取决于螺旋的相互取向。在螺旋-螺旋组装中，由吸引蛋白质-溶剂相互作用的变化引起的焓变化有利于拆卸。在螺旋配对以及，有利的蛋白质分子内相互作用被发现是一样重要的水合作用。总体而言，亲水性蛋白质-溶剂相互作用和蛋白质分子内相互作用被发现在所研究的系统中的折叠和组装的热力学中起着重要的作用。
For a model deca-alanine peptide the cavity (ideal hydrophobic) contribution to hydration favors the helix state over extended states and the paired helix bundle in the assembly of two helices. The energetic contributions of attractive protein–solvent interactions are separated into quasi-chemical components consisting of a short-range part arising from interactions with solvent in the first hydration shell and the remaining long-range part that is well described by a Gaussian. In the helix–coil transition, short-range attractive protein–solvent interactions outweigh hydrophobic hydration and favor the extended coil states. Analysis of enthalpic effects shows that it is the favorable hydration of the peptide backbone that favors the unfolded state. Protein intramolecular interactions favor the helix state and are decisive in favoring folding. In the pairing of two helices, the cavity contribution outweighs the short-range attractive protein–water interactions. However, long-range, protein–solvent attractive interactions can either enhance or reverse this trend depending on the mutual orientation of the helices. In helix–helix assembly, change in enthalpy arising from change in attractive protein–solvent interactions favors disassembly. In helix pairing as well, favorable protein intramolecular interactions are found to be as important as hydration effects. Overall, hydrophilic protein–solvent interactions and protein intramolecular interactions are found to play a significant role in the thermodynamics of folding and assembly in the system studied.
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DOI：
10.1063/1.3532939
发表时间：
2010-10
期刊：
The Journal of chemical physics
影响因子：
--
作者：
P. Varilly;Amish J. Patel;D. Chandler
通讯作者：
P. Varilly;Amish J. Patel;D. Chandler
影响因子：
5.5
作者：
Best, Robert B.;Zhu, Xiao;Shim, Jihyun;Lopes, Pedro E. M.;Mittal, Jeetain;Feig, Michael;MacKerell, Alexander D., Jr.
通讯作者：
MacKerell, Alexander D., Jr.
影响因子：
15
作者：
Kokubo H;Hu CY;Pettitt BM
通讯作者：
Pettitt BM
量热法测定水中丙氨酸肽从 α 螺旋到卷曲转变的焓变。
DOI：
10.1073/pnas.88.7.2854
发表时间：
1991
影响因子：
11.1
作者：
Scholtz,JM;Marqusee,S;Baldwin,RL;York,EJ;Stewart,JM;Santoro,M;Bolen,DW
通讯作者：
Bolen,DW
丙氨酸肽的溶剂化自由能：灵活性的影响。
DOI：
10.1021/jp409693p
发表时间：
2013
期刊：
The journal of physical chemistry. B
影响因子：
--
作者：
Kokubo,Hironori;Harris,RobertC;Asthagiri,Dilipkumar;Pettitt,BMontgomery
通讯作者：
Pettitt,BMontgomery