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本文引用的文献

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Phosphorylation on histidine is accompanied by localized structural changes in the phosphocarrier protein, HPr from Bacillus subtilis.组氨酸磷酸化伴随着来自枯草芽孢杆菌的磷酸载体蛋白HPr的局部结构变化。
Protein Sci. 1997 Oct;6(10):2107-19. doi: 10.1002/pro.5560061006.
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Mapping of the binding interfaces of the proteins of the bacterial phosphotransferase system, HPr and IIAglc.细菌磷酸转移酶系统中蛋白质HPr和IIAglc的结合界面图谱绘制
Biochemistry. 1993 Jan 12;32(1):32-7. doi: 10.1021/bi00052a006.
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The NMR determination of the IIA(mtl) binding site on HPr of the Escherichia coli phosphoenol pyruvate-dependent phosphotransferase system.核磁共振法测定大肠杆菌磷酸烯醇丙酮酸依赖性磷酸转移酶系统中HPr上IIA(mtl)的结合位点。
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Functional interactions between proteins of the phosphoenolpyruvate:sugar phosphotransferase systems of Bacillus subtilis and Escherichia coli.枯草芽孢杆菌和大肠杆菌磷酸烯醇丙酮酸：糖磷酸转移酶系统中蛋白质之间的功能相互作用。
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通过核磁共振化学位移映射展示蛋白质-蛋白质相互作用特异性

Demonstration of protein-protein interaction specificity by NMR chemical shift mapping.

作者信息

Rajagopal P, Waygood E B, Reizer J, Saier M H, Klevit R E

机构信息

University of Washington, Biomolecular Structure Center, Seattle, Washington 98195-7742, USA.

出版信息

Protein Sci. 1997 Dec;6(12):2624-7. doi: 10.1002/pro.5560061214.

DOI:10.1002/pro.5560061214
PMID:9416611
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2143627/
Abstract

Chemical shift mapping is becoming a popular method for studying protein-protein interactions in solution. The technique is used to identify putative sites of interaction on a protein surface by detecting chemical shift perturbations in simple (1H, 15N)-HSQC NMR spectra of a uniformly labeled protein as a function of added (unlabeled) target protein. The high concentrations required for these experiments raise questions concerning the possibility for non-specific interactions being detected, thereby compromising the information obtained. We demonstrate here that the simple chemical shift mapping approach faithfully reproduces the known functional specificities among pairs of closely related proteins from the phosphoenolpyruvate:sugar phosphotransferase systems of Escherichia coli and Bacillus subtilis.

摘要

化学位移图谱正成为研究溶液中蛋白质-蛋白质相互作用的一种常用方法。该技术通过检测均匀标记蛋白质的简单（1H，15N）-HSQC NMR谱中化学位移扰动，作为添加（未标记）靶蛋白的函数，来识别蛋白质表面的假定相互作用位点。这些实验所需的高浓度引发了关于检测到非特异性相互作用的可能性的问题，从而影响所获得的信息。我们在此证明，简单的化学位移图谱方法忠实地再现了来自大肠杆菌和枯草芽孢杆菌磷酸烯醇丙酮酸：糖磷酸转移酶系统的密切相关蛋白质对之间已知的功能特异性。