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Simulations of beta-hairpin folding confined to spherical pores using distributed computing.利用分布式计算对局限于球形孔中的β-发夹折叠进行模拟。
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Residual electrostatic effects in the unfolded state of the N-terminal domain of L9 can be attributed to nonspecific nonlocal charge-charge interactions.L9 N端结构域未折叠状态下的残余静电效应可归因于非特异性非局部电荷-电荷相互作用。
Biochemistry. 2002 May 21;41(20):6533-8. doi: 10.1021/bi025580m.
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A Gaussian-chain model for treating residual charge-charge interactions in the unfolded state of proteins.一种用于处理蛋白质未折叠状态下残余电荷-电荷相互作用的高斯链模型。
Proc Natl Acad Sci U S A. 2002 Mar 19;99(6):3569-74. doi: 10.1073/pnas.052030599. Epub 2002 Mar 12.
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Model for calculation of electrostatic interactions in unfolded proteins.未折叠蛋白质中静电相互作用的计算模型。
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Stabilization of proteins in confined spaces.受限空间中蛋白质的稳定性
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Persistence of native-like topology in a denatured protein in 8 M urea.在8M尿素中变性蛋白质中类天然拓扑结构的持久性。
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Calculation of ensembles of structures representing the unfolded state of an SH3 domain.代表SH3结构域未折叠状态的结构集合的计算。
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pH dependence of stability of staphylococcal nuclease: evidence of substantial electrostatic interactions in the denatured state.葡萄球菌核酸酶稳定性的pH依赖性：变性状态下大量静电相互作用的证据。
Biochemistry. 2000 Nov 21;39(46):14292-304. doi: 10.1021/bi001015c.
9
Charge-charge interactions influence the denatured state ensemble and contribute to protein stability.电荷-电荷相互作用影响变性态系综并有助于蛋白质稳定性。
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NMR characterization of residual structure in the denatured state of protein L.蛋白质L变性状态下残余结构的核磁共振表征
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未折叠的葡萄球菌核酸酶中的残余电荷相互作用可用高斯链模型来解释。

Residual charge interactions in unfolded staphylococcal nuclease can be explained by the Gaussian-chain model.

作者信息

Zhou Huan-Xiang

机构信息

Department of Physics, Drexel University, Philadelphia, PA 19104, USA.

出版信息

Biophys J. 2002 Dec;83(6):2981-6. doi: 10.1016/S0006-3495(02)75304-6.

DOI:10.1016/S0006-3495(02)75304-6
PMID:12496071
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1302379/
Abstract

The discrepancy of the pH dependence of the unfolding free energy for staphylococcal nuclease from what is expected from an idealized model for the unfolded state is accounted for by the recently developed Gaussian-chain model. Residual electrostatic effects in the unfolded state are attributed to nonspecific interactions dominated by charges close along the sequence. The dominance of nonspecific local interactions appears to be supported by some experimental evidence.

摘要

葡萄球菌核酸酶解折叠自由能的pH依赖性与未折叠状态理想化模型预期结果之间的差异，可由最近发展的高斯链模型来解释。未折叠状态下的残余静电效应归因于由序列上相邻电荷主导的非特异性相互作用。非特异性局部相互作用的主导地位似乎得到了一些实验证据的支持。