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关于GroEL伴侣蛋白与蛋白质相互作用的数据集。

Dataset concerning GroEL chaperonin interaction with proteins.

作者信息

Marchenkov V V, Marchenko N Yu, Kaysheva A L, Kotova N V, Kashparov I A, Semisotnov G V

机构信息

Institute of Protein Research, RAS, Russia.

出版信息

Data Brief. 2016 Jan 13;6:619-24. doi: 10.1016/j.dib.2016.01.008. eCollection 2016 Mar.

DOI:10.1016/j.dib.2016.01.008
PMID:26909376
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC4735476/
Abstract

GroEL chaperonin is well-known to interact with a wide variety of polypeptide chains. Here we show the data related to our previous work (http://dx.doi.org/10.1016/j.pep.2015.11.020[1]), and concerning the interaction of GroEL with native (lysozyme, α-lactalbumin) and denatured (lysozyme, α-lactalbumin and pepsin) proteins in solution. The use of affinity chromatography on the base of denatured pepsin for GroEL purification from fluorescent impurities is represented as well.

摘要

众所周知，伴侣蛋白GroEL可与多种多肽链相互作用。在此，我们展示了与我们之前的工作（http://dx.doi.org/10.1016/j.pep.2015.11.020[1]）相关的数据，这些数据涉及GroEL与溶液中的天然蛋白（溶菌酶、α-乳白蛋白）和变性蛋白（溶菌酶、α-乳白蛋白和胃蛋白酶）之间的相互作用。同时还介绍了基于变性胃蛋白酶的亲和色谱法用于从荧光杂质中纯化GroEL的方法。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8049/4735476/2beec4bc9a92/gr4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8049/4735476/c075f33ae6ca/gr1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8049/4735476/2a45dc8980e0/gr2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8049/4735476/42c59a5e4a2e/gr3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8049/4735476/2beec4bc9a92/gr4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8049/4735476/c075f33ae6ca/gr1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8049/4735476/2a45dc8980e0/gr2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8049/4735476/42c59a5e4a2e/gr3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8049/4735476/2beec4bc9a92/gr4.jpg

相似文献

1
Dataset concerning GroEL chaperonin interaction with proteins.关于GroEL伴侣蛋白与蛋白质相互作用的数据集。
Data Brief. 2016 Jan 13;6:619-24. doi: 10.1016/j.dib.2016.01.008. eCollection 2016 Mar.
2
Analysis of interaction between chaperonin GroEL and its substrate using fluorescence correlation spectroscopy.利用荧光相关光谱法分析伴侣蛋白GroEL与其底物之间的相互作用。
Cytometry. 1999 Jul 1;36(3):247-53. doi: 10.1002/(sici)1097-0320(19990701)36:3<247::aid-cyto15>3.3.co;2-r.
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Affinity chromatography of GroEL chaperonin based on denatured proteins: role of electrostatic interactions in regulation of GroEL affinity for protein substrates.基于变性蛋白的伴侣蛋白GroEL亲和层析：静电相互作用在调节GroEL对蛋白质底物亲和力中的作用
Biochemistry (Mosc). 2006 Dec;71(12):1357-64. doi: 10.1134/s000629790612011x.
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Back to GroEL-Assisted Protein Folding: GroES Binding-Induced Displacement of Denatured Proteins from GroEL to Bulk Solution.回到 GroEL 辅助蛋白折叠：GroES 结合诱导变性蛋白从 GroEL 到体相溶液的置换。
Biomolecules. 2020 Jan 20;10(1):162. doi: 10.3390/biom10010162.
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Calorimetric observation of a GroEL-protein binding reaction with little contribution of hydrophobic interaction.对GroEL-蛋白质结合反应进行的量热法观察，其中疏水相互作用的贡献很小。
J Biol Chem. 1997 Dec 19;272(51):32158-62. doi: 10.1074/jbc.272.51.32158.
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Chaperonin-affected refolding of alpha-lactalbumin: effects of nucleotides and the co-chaperonin GroES.伴侣素对α-乳白蛋白重折叠的影响：核苷酸和共伴侣素GroES的作用
J Mol Biol. 1999 Oct 15;293(1):125-37. doi: 10.1006/jmbi.1999.3142.
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Mechanisms for GroEL/GroES-mediated folding of a large 86-kDa fusion polypeptide in vitro.体外GroEL/GroES介导的86 kDa大融合多肽折叠机制。
J Biol Chem. 1999 Apr 9;274(15):10405-12. doi: 10.1074/jbc.274.15.10405.
8
[Effect of ADP and GroES on interaction of molecular chaperonin GroEL with non-native lysozyme].[二磷酸腺苷（ADP）和伴侣蛋白GroES对分子伴侣蛋白GroEL与非天然溶菌酶相互作用的影响]
Ukr Biokhim Zh (1999). 2003 May-Jun;75(3):88-94.
9
Kinetic analysis of interactions between GroEL and reduced alpha-lactalbumin. Effect of GroES and nucleotides.GroEL与还原型α-乳白蛋白相互作用的动力学分析。GroES和核苷酸的作用。
J Biol Chem. 1995 Aug 25;270(34):19957-63. doi: 10.1074/jbc.270.34.19957.
10
The chaperonin GroEL does not recognize apo-alpha-lactalbumin in the molten globule state.伴侣蛋白GroEL无法识别处于熔球态的脱辅基α-乳白蛋白。
Nat Struct Biol. 1994 Jul;1(7):439-46. doi: 10.1038/nsb0794-439.

本文引用的文献

1
Affinity chromatography of chaperones based on denatured proteins: Analysis of cell lysates of different origin.基于变性蛋白的伴侣蛋白亲和层析：不同来源细胞裂解物的分析
Protein Expr Purif. 2016 Mar;119:117-23. doi: 10.1016/j.pep.2015.11.020. Epub 2015 Nov 28.
2
Synchrotron small-angle X-ray scattering studies of the structure of porcine pepsin under various pH conditions.同步加速器小角X射线散射研究不同pH条件下猪胃蛋白酶的结构
J Phys Chem B. 2008 Dec 11;112(49):15821-7. doi: 10.1021/jp805940d.
3
Affinity chromatography of GroEL chaperonin based on denatured proteins: role of electrostatic interactions in regulation of GroEL affinity for protein substrates.
基于变性蛋白的伴侣蛋白GroEL亲和层析：静电相互作用在调节GroEL对蛋白质底物亲和力中的作用
Biochemistry (Mosc). 2006 Dec;71(12):1357-64. doi: 10.1134/s000629790612011x.
4
Analysis of interaction between chaperonin GroEL and its substrate using fluorescence correlation spectroscopy.利用荧光相关光谱法分析伴侣蛋白GroEL与其底物之间的相互作用。
Cytometry. 1999 Jul 1;36(3):247-53. doi: 10.1002/(sici)1097-0320(19990701)36:3<247::aid-cyto15>3.3.co;2-r.
5
Calorimetric observation of a GroEL-protein binding reaction with little contribution of hydrophobic interaction.对GroEL-蛋白质结合反应进行的量热法观察，其中疏水相互作用的贡献很小。
J Biol Chem. 1997 Dec 19;272(51):32158-62. doi: 10.1074/jbc.272.51.32158.
6
Mechanism of GroEL action: productive release of polypeptide from a sequestered position under GroES.GroEL作用机制：多肽从GroES下方的隔离位置有效释放。
Cell. 1995 Nov 17;83(4):577-87. doi: 10.1016/0092-8674(95)90098-5.
7
(Mg-ATP)-dependent self-assembly of molecular chaperone GroEL.分子伴侣GroEL的（Mg-ATP）依赖性自组装
Nature. 1990 Nov 22;348(6299):339-42. doi: 10.1038/348339a0.
8
The aromatic amino acid content of the bacterial chaperone protein groEL (cpn60). Evidence for the presence of a single tryptophan.细菌伴侣蛋白groEL（cpn60）的芳香族氨基酸含量。存在单个色氨酸的证据。
FEBS Lett. 1991 Nov 4;292(1-2):9-12. doi: 10.1016/0014-5793(91)80821-j.
9
An improved assay for nanomole amounts of inorganic phosphate.一种用于检测纳摩尔量无机磷酸盐的改进测定法。
Anal Biochem. 1979 Nov 15;100(1):95-7. doi: 10.1016/0003-2697(79)90115-5.