气候变化领域集成服务门户(CCPortal): Quantifying and visualizing weak interactions between anions and proteins

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DOI	10.1073/pnas.2015879118
	Quantifying and visualizing weak interactions between anions and proteins
	Yu B.; Pletka C.C.; Iwahara J.
发表日期	2021
ISSN	00278424
卷号	118 期号:2
英文摘要	The molecular properties of proteins are influenced by various ions present in the same solution. While site-specific strong interactions between multivalent metal ions and proteins are well characterized, the behavior of other ions that are only weakly interacting with proteins remains elusive. In the current study, using NMR spectroscopy, we have investigated anion-protein interactions for three proteins that are similar in size but differ in overall charge. Using a unique NMR-based approach, we quantified anions accumulated around the proteins. The determined numbers of anions that are electrostatically attracted to the charged proteins were notably smaller than the overall charge valences and were consistent with predictions from the Poisson-Boltzmann theory. This NMR-based approach also allowed us to measure ionic diffusion and characterize the anions interacting with the positively charged proteins. Our data show that these anions rapidly diffuse while bound to the proteins. Using the same experimental approach, we observed the release of the anions from the protein surface upon the formation of the Antp homeodomain-DNA complex. Using paramagnetic relaxation enhancement (PRE), we visualized the spatial distribution of anions around the free proteins and the Antp homeodomain-DNA complex. The obtained PRE data revealed the localization of anions in the vicinity of the highly positively charged regions of the free Antp homeodomain and provided further evidence of the release of anions from the protein surface upon the protein-DNA association. This study sheds light on the dynamic behavior of anions that electrostatically interact with proteins. © This open access article is distributed under Creative Commons Attribution-NonCommercial-NoDerivatives License 4.0 (CC BY-NC-ND).
英文关键词	Dynamics; Electrostatic interactions; Ions; Nuclear magnetic resonance; Proteins
语种	英语
scopus关键词	metal ion; anion protein interaction; anion release; Antp homeodomain; Article; charge valence; chemical analysis; chemical interaction; chemical parameters; chemical phenomena; chemical procedures; chemical reaction; complex formation; controlled study; DNA structure; electrical parameters; ionic diffusion; nuclear magnetic resonance spectroscopy; paramagnetic relaxation enhancement; Poisson Boltzmann theory; priority journal; protein DNA interaction; protein engineering; protein interaction; protein localization; spatial distribution; static electricity; theory; thermodynamics
来源期刊	Proceedings of the National Academy of Sciences of the United States of America
文献类型	期刊论文
条目标识符	http://gcip.llas.ac.cn/handle/2XKMVOVA/181045
作者单位	Department of Biochemistry and Molecular Biology, Sealy Center for Structural Biology and Molecular Biophysics, University of Texas, Medical Branch, Galveston, TX 77555-1068, United States
推荐引用方式 GB/T 7714	Yu B.,Pletka C.C.,Iwahara J.. Quantifying and visualizing weak interactions between anions and proteins[J],2021,118(2).
APA	Yu B.,Pletka C.C.,&Iwahara J..(2021).Quantifying and visualizing weak interactions between anions and proteins.Proceedings of the National Academy of Sciences of the United States of America,118(2).
MLA	Yu B.,et al."Quantifying and visualizing weak interactions between anions and proteins".Proceedings of the National Academy of Sciences of the United States of America 118.2(2021).