气候变化领域集成服务门户(CCPortal): Structure, self-assembly, and properties of a truncated reflectin variant

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DOI	10.1073/PNAS.2009044117
	Structure, self-assembly, and properties of a truncated reflectin variant
	Umerani M.J.; Pratakshya P.; Chatterjee A.; Cerna Sanchez J.A.; Kim H.S.; Ilc G.; Kovačič M.; Magnan C.; Marmiroli B.; Sartori B.; Kwansa A.L.; Orins H.; Bartlett A.W.; Leung E.M.; Feng Z.; Naughton K.L.; Norton-Baker B.; Phan L.; Long J.; Allevato A.; Leal-Cruz J.E.; Lin Q.; Baldi P.; Bernstorff S.; Plavec J.; Yingling Y.G.; Gorodetsky A.A.
发表日期	2021
ISSN	00278424
起始页码	32891
结束页码	32901
卷号	117 期号:52
英文摘要	Naturally occurring and recombinant protein-based materials are frequently employed for the study of fundamental biological processes and are often leveraged for applications in areas as diverse as electronics, optics, bioengineering, medicine, and even fashion. Within this context, unique structural proteins known as reflectins have recently attracted substantial attention due to their key roles in the fascinating color-changing capabilities of cephalopods and their technological potential as biophotonic and bioelectronic materials. However, progress toward understanding reflectins has been hindered by their atypical aromatic and charged residue-enriched sequences, extreme sensitivities to subtle changes in environmental conditions, and well-known propensities for aggregation. Herein, we elucidate the structure of a reflectin variant at the molecular level, demonstrate a straightforward mechanical agitation-based methodology for controlling this variant’s hierarchical assembly, and establish a direct correlation between the protein’s structural characteristics and intrinsic optical properties. Altogether, our findings address multiple challenges associated with the development of reflectins as materials, furnish molecular-level insight into the mechanistic underpinnings of cephalopod skin cells’ color-changing functionalities, and may inform new research directions across biochemistry, cellular biology, bioengineering, and optics. © 2020 National Academy of Sciences. All rights reserved.
英文关键词	Biomaterials; Optical properties; Proteins; Reflectin; Self-assembly
语种	英语
scopus关键词	agitation; article; biochemistry; bioengineering; cephalopod; human cell; nonhuman; optics; skin cell
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/179601
作者单位	Department of Materials Science and Engineering, University of California, Irvine, CA 92697, United States; Department of Chemistry, University of California, Irvine, CA 92697, United States; Department of Chemical and Biomolecular Engineering, University of California, Irvine, CA 92697, United States; Department of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697, United States; Department of Materials Science and Engineering, North Carolina State University, Raleigh, NC 27695, United States; Slovenian NMR Centre, National Institute of Chemistry, Ljubljana, 1000, Slovenia; Department of Computer Science, University of California, Irvine, CA 92697, United States; Institute of Inorganic Chemistry, Graz University of Technology, Graz, 8010, Austria; Department of Physics and Astronomy, University of California, Irvine, CA 92697, United States; Irvine Materials Research Institute, University of California, Irvine, CA 92697, United States; Elettra–Sincrotrone Trieste, Tri...
推荐引用方式 GB/T 7714	Umerani M.J.,Pratakshya P.,Chatterjee A.,et al. Structure, self-assembly, and properties of a truncated reflectin variant[J],2021,117(52).
APA	Umerani M.J..,Pratakshya P..,Chatterjee A..,Cerna Sanchez J.A..,Kim H.S..,...&Gorodetsky A.A..(2021).Structure, self-assembly, and properties of a truncated reflectin variant.Proceedings of the National Academy of Sciences of the United States of America,117(52).
MLA	Umerani M.J.,et al."Structure, self-assembly, and properties of a truncated reflectin variant".Proceedings of the National Academy of Sciences of the United States of America 117.52(2021).