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Conformations of peptoids in nanosheets result from the interplay of backbone energetics and intermolecular interactions

Journal Article · · Proceedings of the National Academy of Sciences of the United States of America
 [1];  [2];  [3];  [4];  [5];  [4];  [1];  [1]
  1. Molecular Foundry, Lawrence Berkeley National Laboratory, Berkeley, CA 94720,
  2. Molecular Foundry, Lawrence Berkeley National Laboratory, Berkeley, CA 94720,, Department of Chemical Engineering &, Materials Science, University of California, Irvine, Irvine, CA 92697,
  3. Center for Genomics and Systems Biology, New York University Abu Dhabi, Abu Dhabi, United Arab Emirates,
  4. School of Chemical &, Biomolecular Engineering, Georgia Institute of Technology, Atlanta, GA 30332
  5. Department of Chemical Engineering &, Materials Science, University of California, Irvine, Irvine, CA 92697,

Significance

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.

Sponsoring Organization:
USDOE
Grant/Contract Number:
AC02-05CH11231
OSTI ID:
1437093
Journal Information:
Proceedings of the National Academy of Sciences of the United States of America, Journal Name: Proceedings of the National Academy of Sciences of the United States of America Journal Issue: 22 Vol. 115; ISSN 0027-8424
Publisher:
Proceedings of the National Academy of SciencesCopyright Statement
Country of Publication:
United States
Language:
English

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