气候变化领域集成服务门户(CCPortal): Ice-nucleating proteins are activated by low temperatures to control the structure of interfacial water

CCPortal

DOI	10.1038/s41467-021-21349-3
	Ice-nucleating proteins are activated by low temperatures to control the structure of interfacial water
	Roeters S.J.; Golbek T.W.; Bregnhøj M.; Drace T.; Alamdari S.; Roseboom W.; Kramer G.; Šantl-Temkiv T.; Finster K.; Pfaendtner J.; Woutersen S.; Boesen T.; Weidner T.
发表日期	2021
ISSN	2041-1723
卷号	12 期号:1
英文摘要	Ice-nucleation active (INA) bacteria can promote the growth of ice more effectively than any other known material. Using specialized ice-nucleating proteins (INPs), they obtain nutrients from plants by inducing frost damage and, when airborne in the atmosphere, they drive ice nucleation within clouds, which may affect global precipitation patterns. Despite their evident environmental importance, the molecular mechanisms behind INP-induced freezing have remained largely elusive. We investigate the structural basis for the interactions between water and the ice-nucleating protein InaZ from the INA bacterium Pseudomonas syringae. Using vibrational sum-frequency generation (SFG) and two-dimensional infrared spectroscopy, we demonstrate that the ice-active repeats of InaZ adopt a β-helical structure in solution and at water surfaces. In this configuration, interaction between INPs and water molecules imposes structural ordering on the adjacent water network. The observed order of water increases as the interface is cooled to temperatures close to the melting point of water. Experimental SFG data combined with molecular-dynamics simulations and spectral calculations show that InaZ reorients at lower temperatures. This reorientation can enhance water interactions, and thereby the effectiveness of ice nucleation. © 2021, The Author(s).
语种	英语
scopus关键词	bacterial protein; InaZ protein; unclassified drug; water; deuterium oxide; ice; ice nucleation protein; outer membrane protein; water; bacterium; freezing; low temperature; molecular analysis; nucleation; protein; Article; infrared spectroscopy; low temperature; melting point; molecular dynamics; molecular interaction; nonhuman; Pseudomonas syringae; vibrational sum frequency generation spectroscopy; water structure; atmosphere; chemistry; cold; freezing; genetics; metabolism; microbiology; plant; Pseudomonas syringae; Bacteria (microorganisms); Pseudomonas syringae; Atmosphere; Bacterial Outer Membrane Proteins; Cold Temperature; Deuterium Oxide; Freezing; Ice; Molecular Dynamics Simulation; Plants; Pseudomonas syringae; Water
来源期刊	Nature Communications
文献类型	期刊论文
条目标识符	http://gcip.llas.ac.cn/handle/2XKMVOVA/251508
作者单位	Department of Chemistry, Aarhus University, Aarhus C, Denmark; Van ‘t Hoff Institute for Molecular Sciences, University of Amsterdam, Amsterdam, Netherlands; Department of Molecular Biology and Genetics, Aarhus University, Aarhus C, Denmark; Department of Chemical Engineering, University of Washington, Seattle, WA, United States; Swammerdam Institute for Life Sciences, University of Amsterdam, Amsterdam, Netherlands; Department of Biology, Aarhus University, Aarhus C, Denmark; The Stellar Astrophysics Centre – SAC, Department of Physics and Astronomy, Aarhus University, Aarhus C, Denmark; Interdisciplinary Nanoscience Center – iNano, Aarhus University, Aarhus C, Denmark
推荐引用方式 GB/T 7714	Roeters S.J.,Golbek T.W.,Bregnhøj M.,et al. Ice-nucleating proteins are activated by low temperatures to control the structure of interfacial water[J],2021,12(1).
APA	Roeters S.J..,Golbek T.W..,Bregnhøj M..,Drace T..,Alamdari S..,...&Weidner T..(2021).Ice-nucleating proteins are activated by low temperatures to control the structure of interfacial water.Nature Communications,12(1).
MLA	Roeters S.J.,et al."Ice-nucleating proteins are activated by low temperatures to control the structure of interfacial water".Nature Communications 12.1(2021).