Long proteins with unique optimal foldings in the H-P model

Long proteins with unique optimal foldings in the H-P model

It is widely accepted that (1) the natural or folded state of proteins is a global energy minimum, and (2) in most cases proteins fold to a unique state determined by their amino acid sequence. The H-P (hydrophobic-hydrophilic) model is a simple combinatorial model designed to answer qualitative que...

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Bibliographic Details
Main Authors: Aichholzer, Oswin, Bremner, David, Demaine, Erik D., Meijer, Henk, Sacristán, Vera, Soss, Michael
Other Authors: Massachusetts Institute of Technology. Department of Electrical Engineering and Computer Science
Format: Article
Language:en_US
Published: Elsevier 2014
Online Access:http://hdl.handle.net/1721.1/86069
https://orcid.org/0000-0003-3803-5703

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http://hdl.handle.net/1721.1/86069
https://orcid.org/0000-0003-3803-5703

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