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评论“Innovative scattering analysis shows that hydrophobic disordered proteins are expanded in water”。

Comment on "Innovative scattering analysis shows that hydrophobic disordered proteins are expanded in water".

机构信息

Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, Bethesda, MD 20892, USA.

College of Integrative Sciences and Arts, Arizona State University, Mesa, AZ 85212, USA.

出版信息

Science. 2018 Aug 31;361(6405). doi: 10.1126/science.aar7101.

DOI:10.1126/science.aar7101
PMID:30166459
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC7507683/
Abstract

Riback (Reports, 13 October 2017, p. 238) used small-angle x-ray scattering (SAXS) experiments to infer a degree of compaction for unfolded proteins in water versus chemical denaturant that is highly consistent with the results from Förster resonance energy transfer (FRET) experiments. There is thus no "contradiction" between the two methods, nor evidence to support their claim that commonly used FRET fluorophores cause protein compaction.

摘要

Riback(报道,2017 年 10 月 13 日,第 238 页)利用小角 X 射线散射(SAXS)实验推断了在水中和化学变性剂中展开蛋白质的紧凑程度,这与Förster 共振能量转移(FRET)实验的结果高度一致。因此,这两种方法之间没有“矛盾”,也没有证据支持他们的说法,即常用的 FRET 荧光染料会导致蛋白质紧凑。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/83ac/7507683/707d2fd874ec/nihms-1626250-f0002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/83ac/7507683/88552ae9cd78/nihms-1626250-f0001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/83ac/7507683/707d2fd874ec/nihms-1626250-f0002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/83ac/7507683/88552ae9cd78/nihms-1626250-f0001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/83ac/7507683/707d2fd874ec/nihms-1626250-f0002.jpg

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本文引用的文献

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Innovative scattering analysis shows that hydrophobic disordered proteins are expanded in water.创新的散射分析表明,疏水无序蛋白在水中会膨胀。
Science. 2017 Oct 13;358(6360):238-241. doi: 10.1126/science.aan5774.
2
Decoupling of size and shape fluctuations in heteropolymeric sequences reconciles discrepancies in SAXS vs. FRET measurements.杂多序列中大小和形状波动的解耦调和了 SAXS 与 FRET 测量之间的差异。
Proc Natl Acad Sci U S A. 2017 Aug 1;114(31):E6342-E6351. doi: 10.1073/pnas.1704692114. Epub 2017 Jul 17.
3
Probing the Action of Chemical Denaturant on an Intrinsically Disordered Protein by Simulation and Experiment.
使用反常X射线散射干涉测量法测定蛋白质中的绝对分子内距离。
Nanoscale. 2025 Feb 6;17(6):3322-3330. doi: 10.1039/d4nr03375b.
4
A genetically encoded anomalous SAXS ruler to probe the dimensions of intrinsically disordered proteins.一种用于探测内在无序蛋白质尺寸的基因编码异常小角X射线散射标尺。
Proc Natl Acad Sci U S A. 2024 Dec 10;121(50):e2415220121. doi: 10.1073/pnas.2415220121. Epub 2024 Dec 6.
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Critical Assessment of Self-Consistency Checks in the All-Atom Molecular Dynamics Simulation of Intrinsically Disordered Proteins.无偏分子动力学模拟中内源性无序蛋白自一致性检验的关键性评估
J Chem Theory Comput. 2023 May 23;19(10):2973-2984. doi: 10.1021/acs.jctc.2c01140. Epub 2023 May 3.
6
The Protein Unfolded State: One, No One and One Hundred Thousand.蛋白质去折叠状态:一、非一和千千万万。
J Am Chem Soc. 2022 Dec 14;144(49):22352-22357. doi: 10.1021/jacs.2c07696. Epub 2022 Nov 30.
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The biophysics of disordered proteins from the point of view of single-molecule fluorescence spectroscopy.从单分子荧光光谱学的角度看无序蛋白质的生物物理学。
Essays Biochem. 2022 Dec 16;66(7):875-890. doi: 10.1042/EBC20220065.
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