Structure, self-assembly, and properties of a truncated reflectin variant
Abstract
The investigation of protein-based materials has provided a better understanding of living systems and has led to the development of ubiquitous modern technologies. Within this context, unique cephalopod proteins called reflectins have exhibited promise for biophotonics and bioelectronics applications, but the exploration of reflectins as materials has been hindered by an incomplete understanding of their structures and properties. Here, we resolve the molecular-level structure of a model reflectin variant, establish a straightforward approach to controlling the assembly of this protein, and describe a correlation between its structural characteristics and light-manipulating properties. Taken together, our findings advance current understanding of reflectin-based materials, provide insight into the color-changing capabilities of cephalopods, and afford new opportunities in biochemistry, cellular biology, bioengineering, and optics.
Document Details
- Document Type
- Pub Defense Publication
- Publication Date
- Dec 15, 2020
- Source ID
- 10.1073/pnas.2009044117
Entities
People
- Albert L. Kwansa
- Alex Allevato
- Alon A. Gorodetsky
- Andrew W. Bartlett
- Atrouli Chatterjee
- Barbara Sartori
- Benedetta Marmiroli
- Brenna Norton-baker
- Christophe Magnan
- Erica M. Leung
- Gregor Ilc
- Helen Orins
- Ho Shin Kim
- James M. Long
- Janez Plavec
- Jessica E. Leal-cruz
- Juana A. Cerna Sanchez
- Kyle L. Naughton
- Long Phan
- Matic Kovačič
- Mehran J. Umerani
- Pierre Baldi
- Preeta Pratakshya
- Qiyin Lin
- Sigrid Bernstorff
- Yaroslava G. Yingling
- Zhijing Feng
Organizations
- Air Force Office of Scientific Research
- ELETTRA
- Graz University of Technology
- National Institute of Chemistry
- North Carolina State University
- University of California