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质量很重要：具有良好疏水接触的残基簇的扩展稳定（超）嗜热蛋白质。

Quality matters: extension of clusters of residues with good hydrophobic contacts stabilize (hyper)thermophilic proteins.

机构信息

Institute for Pharmaceutical and Medicinal Chemistry, Department of Mathematics and Natural Sciences, Heinrich Heine University , Universitätsstr. 1, 40225 Düsseldorf, Germany.

出版信息

J Chem Inf Model. 2014 Feb 24;54(2):355-61. doi: 10.1021/ci400568c. Epub 2014 Jan 28.

DOI:10.1021/ci400568c
PMID:24437522
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3985445/
Abstract

Identifying determinant(s) of protein thermostability is key for rational and data-driven protein engineering. By analyzing more than 130 pairs of mesophilic/(hyper)thermophilic proteins, we identified the quality (residue-wise energy) of hydrophobic interactions as a key factor for protein thermostability. This distinguishes our study from previous ones that investigated predominantly structural determinants. Considering this key factor, we successfully discriminated between pairs of mesophilic/(hyper)thermophilic proteins (discrimination accuracy: ∼80%) and searched for structural weak spots in E. coli dihydrofolate reductase (classification accuracy: 70%).

摘要

确定蛋白质热稳定性的决定因素对于理性和数据驱动的蛋白质工程至关重要。通过分析超过 130 对嗜温/(超)嗜热蛋白质，我们确定了疏水相互作用的质量（残基能量）是蛋白质热稳定性的关键因素。这使我们的研究与以前主要研究结构决定因素的研究区分开来。考虑到这个关键因素，我们成功地区分了嗜温/(超)嗜热蛋白质对（区分准确性：约 80%），并搜索了大肠杆菌二氢叶酸还原酶的结构弱点（分类准确性：70%）。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5fcb/3985445/a119a393a602/ci-2013-00568c_0005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5fcb/3985445/78222ece6d1b/ci-2013-00568c_0002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5fcb/3985445/00c4bc7d0677/ci-2013-00568c_0003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5fcb/3985445/ca9e54ee9f90/ci-2013-00568c_0004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5fcb/3985445/a119a393a602/ci-2013-00568c_0005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5fcb/3985445/78222ece6d1b/ci-2013-00568c_0002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5fcb/3985445/00c4bc7d0677/ci-2013-00568c_0003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5fcb/3985445/ca9e54ee9f90/ci-2013-00568c_0004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5fcb/3985445/a119a393a602/ci-2013-00568c_0005.jpg

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Thermostabilizing mutations preferentially occur at structural weak spots with a high mutation ratio.
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