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Fast folding and slow unfolding of a resurrected Precambrian protein.

作者信息

Candel Adela M, Romero-Romero M Luisa, Gamiz-Arco Gloria, Ibarra-Molero Beatriz, Sanchez-Ruiz Jose M

机构信息

Departamento de Quimica Fisica, Facultad de Ciencias, Universidad de Granada, Granada 18071, Spain.

Departamento de Quimica Fisica, Facultad de Ciencias, Universidad de Granada, Granada 18071, Spain

出版信息

Proc Natl Acad Sci U S A. 2017 May 23;114(21):E4122-E4123. doi: 10.1073/pnas.1703227114. Epub 2017 May 16.

DOI:10.1073/pnas.1703227114
PMID:28512228
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC5448177/
Abstract
摘要

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Proc Natl Acad Sci U S A. 2017 Feb 28;114(9):E1627-E1632. doi: 10.1073/pnas.1613892114. Epub 2017 Feb 14.
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Selection for Protein Kinetic Stability Connects Denaturation Temperatures to Organismal Temperatures and Provides Clues to Archaean Life.对蛋白质动力学稳定性的选择将变性温度与生物体温度联系起来，并为太古宙生命提供线索。
PLoS One. 2016 Jun 2;11(6):e0156657. doi: 10.1371/journal.pone.0156657. eCollection 2016.
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Mutational studies on resurrected ancestral proteins reveal conservation of site-specific amino acid preferences throughout evolutionary history.对复活的祖先蛋白质的突变研究揭示了在整个进化历史中位点特异性氨基酸偏好的保守性。
Mol Biol Evol. 2015 Feb;32(2):440-55. doi: 10.1093/molbev/msu312. Epub 2014 Nov 12.
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Conservation of protein structure over four billion years.四十亿年来蛋白质结构的保守性。
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Single-molecule paleoenzymology probes the chemistry of resurrected enzymes.单分子古酶学探测复活酶的化学性质。
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Natural selection for kinetic stability is a likely origin of correlations between mutational effects on protein energetics and frequencies of amino acid occurrences in sequence alignments.对动力学稳定性的自然选择可能是序列比对中突变对蛋白质能量学的影响与氨基酸出现频率之间相关性的一个起源。
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