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假设：蛋白质介电常数的展开力。

Hypothesis: The unfolding power of protein dielectricity.

作者信息

Uversky Vladimir N

机构信息

Department of Molecular Medicine and USF Health Byrd Alzheimer's Research Institute; Morsani College of Medicine; University of South Florida; Tampa, FL USA.

Institute for Biological Instrumentation; Russian Academy of Sciences; Moscow Region, Russia.

出版信息

Intrinsically Disord Proteins. 2013 Jul 11;1(1):e25725. doi: 10.4161/idp.25725. eCollection 2013 Jan-Dec.

DOI:10.4161/idp.25725
PMID:28516018
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC5424796/
Abstract

A hypothesis is proposed on a potential role of protein dielectricity as an unfolding factor in protein-protein interactions. It is suggested that large protein complexes and aggregation seeds can unfold target proteins by virtue of their effect on the dielectric properties of water at the protein-solvent interface. Here, similar to the effect of membrane surfaces, protein surface can cause decrease in the local dielectric constant of solvent and thereby induce structural changes in a target protein approaching this surface. Some potential implementations of this hypothetical mechanism are also discussed.

摘要

提出了一个关于蛋白质介电常数作为蛋白质-蛋白质相互作用中解折叠因子的潜在作用的假说。有人认为，大的蛋白质复合物和聚集种子可以通过其对蛋白质-溶剂界面处水的介电性质的影响来使靶蛋白解折叠。在这里，类似于膜表面的作用，蛋白质表面可导致溶剂的局部介电常数降低，从而在接近该表面的靶蛋白中诱导结构变化。还讨论了这一假说机制的一些潜在应用。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3a26/5424796/9941acf09c7f/kidp-01-01-10925725-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3a26/5424796/fce9acad0159/kidp-01-01-10925725-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3a26/5424796/9941acf09c7f/kidp-01-01-10925725-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3a26/5424796/fce9acad0159/kidp-01-01-10925725-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3a26/5424796/9941acf09c7f/kidp-01-01-10925725-g002.jpg

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2
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Proc Natl Acad Sci U S A. 2013 Mar 5;110(10):3871-6. doi: 10.1073/pnas.1216597110. Epub 2013 Feb 19.
3
PUMA binding induces partial unfolding within BCL-xL to disrupt p53 binding and promote apoptosis.
Intrinsically Disord Proteins. 2013 Jan 1;1(1):e27130. doi: 10.4161/idp.27130. eCollection 2013 Jan-Dec.
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Nat Chem Biol. 2013 Mar;9(3):163-8. doi: 10.1038/nchembio.1166. Epub 2013 Jan 20.
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Mechanical probes of SOD1 predict systematic trends in metal and dimer affinity of ALS-associated mutants.机械探针探测 SOD1，预测 ALS 相关突变体对金属和二聚体亲和力的系统趋势。
J Mol Biol. 2013 Mar 11;425(5):850-74. doi: 10.1016/j.jmb.2012.12.022. Epub 2013 Jan 3.
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Unusual biophysics of intrinsically disordered proteins.内在无序蛋白质的异常生物物理学
Biochim Biophys Acta. 2013 May;1834(5):932-51. doi: 10.1016/j.bbapap.2012.12.008. Epub 2012 Dec 23.
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