气候变化领域集成服务门户(CCPortal): Water follows polar and nonpolar protein surface domains

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DOI	10.1073/pnas.1910225116
	Water follows polar and nonpolar protein surface domains
	Qiao B.; Jiménez-Ángeles F.; Nguyen T.D.; De La Cruz M.O.
发表日期	2019
ISSN	0027-8424
起始页码	19274
结束页码	19281
卷号	116 期号:39
英文摘要	The conformation of water around proteins is of paramount importance, as it determines protein interactions. Although the average water properties around the surface of proteins have been provided experimentally and computationally, protein surfaces are highly heterogeneous. Therefore, it is crucial to determine the correlations of water to the local distributions of polar and nonpolar protein surface domains to understand functions such as aggregation, mutations, and delivery. By using atomistic simulations, we investigate the orientation and dynamics of water molecules next to 4 types of protein surface domains: negatively charged, positively charged, and charge-neutral polar and nonpolar amino acids. The negatively charged amino acids orient around 98% of the neighboring water dipoles toward the protein surface, and such correlation persists up to around 16 A from the protein surface. The positively charged amino acids orient around 94% of the nearest water dipoles against the protein surface, and the correlation persists up to around 12 A. The charge-neutral polar and nonpolar amino acids are also orienting the water neighbors in a quantitatively weaker manner. A similar trend was observed in the residence time of the nearest water neighbors. These findings hold true for 3 technically important enzymes (PETase, cytochrome P450, and organophosphorus hydrolase). Our results demonstrate that the water-amino acid degree of correlation follows the same trend as the amino acid contribution in proteins solubility, namely, the negatively charged amino acids are the most beneficial for protein solubility, then the positively charged amino acids, and finally the charge-neutral amino acids. © 2019 National Academy of Sciences. All rights reserved.
英文关键词	AMOEBA force field; Proteins; Solubility; Surface; Water
语种	英语
scopus关键词	amino acid; aryldialkylphosphatase; cytochrome P450; enzyme; polyethylene terephthalate; protein; protein PETase; unclassified drug; water; Article; controlled study; dipole; mutation; priority journal; protein aggregation; protein domain; protein localization; retention time; solubility; surface property
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/160344
作者单位	Qiao, B., Department of Materials Science and Engineering, Northwestern University, Evanston, IL 60208, United States; Jiménez-Ángeles, F., Department of Materials Science and Engineering, Northwestern University, Evanston, IL 60208, United States; Nguyen, T.D., Department of Chemical and Biological Engineering, Northwestern University, Evanston, IL 60208, United States; De La Cruz, M.O., Department of Materials Science and Engineering, Northwestern University, Evanston, IL 60208, United States, Department of Chemical and Biological Engineering, Northwestern University, Evanston, IL 60208, United States, Department of Chemistry, Northwestern University, Evanston, IL 60208, United States, Department of Physics and Astronomy, Northwestern University, Evanston, IL 60208, United States
推荐引用方式 GB/T 7714	Qiao B.,Jiménez-Ángeles F.,Nguyen T.D.,et al. Water follows polar and nonpolar protein surface domains[J],2019,116(39).
APA	Qiao B.,Jiménez-Ángeles F.,Nguyen T.D.,&De La Cruz M.O..(2019).Water follows polar and nonpolar protein surface domains.Proceedings of the National Academy of Sciences of the United States of America,116(39).
MLA	Qiao B.,et al."Water follows polar and nonpolar protein surface domains".Proceedings of the National Academy of Sciences of the United States of America 116.39(2019).