Conformations of peptoids in nanosheets result from the interplay of backbone energetics and intermolecular interactions
Abstract
Commonly observed secondary structures of proteins, such as α -helices and β -sheets, are built from a trans- amide backbone with residues sampling a single region of the Ramachandran plot. Here we report a secondary structure displayed by biomimetic peptoid polymers in which the backbone exhibits the cis conformation and alternating residues display rotational states of opposed (pseudo)chirality. This structure is linear and untwisted and enables strands to pack densely into extended bilayer nanosheets.
Document Details
- Document Type
- Pub Defense Publication
- Publication Date
- May 14, 2018
- Source ID
- 10.1073/pnas.1800397115
Entities
People
- Allon I Hochbaum
- Anant K Paravastu
- Benjamin C. Hudson
- Glenn L. Butterfoss
- John R. Edison
- Ronald N Zuckermann
- Ryan K Spencer
- Stephen Whitelam
Organizations
- Air Force Office of Scientific Research
- Defense Threat Reduction Agency
- Georgia Tech
- Lawrence Berkeley National Laboratory
- New York University
- United States Department of Energy
- University of California, Irvine