Conformations of peptoids in nanosheets result from the interplay of backbone energetics and intermolecular interactions
| Autor: | Ronald N. Zuckermann, Allon I. Hochbaum, Benjamin C. Hudson, Anant K. Paravastu, Glenn L. Butterfoss, Stephen Whitelam, Ryan K. Spencer, John R. Edison |
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| Rok vydání: | 2018 |
| Předmět: |
Materials science
Molecular model Polymers Peptoid nanosheet 02 engineering and technology Molecular Dynamics Simulation 010402 general chemistry 01 natural sciences Protein Structure Secondary Supramolecular assembly Peptoids Molecular dynamics chemistry.chemical_compound Biomimetic Materials Molecule Nanosheet Multidisciplinary Intermolecular force Peptoid 021001 nanoscience & nanotechnology Nanostructures 0104 chemical sciences chemistry Chemical physics Physical Sciences 0210 nano-technology |
| Zdroj: | Proceedings of the National Academy of Sciences. 115:5647-5651 |
| ISSN: | 1091-6490 0027-8424 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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