Inverse design of proteins with hydrophobic and polar amino acids

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dc.creatorMicheletti, C.
dc.creatorSeno, F.
dc.creatorMaritan, A.
dc.creatorBanavar, J. R.
dc.date1997-12-11
dc.date.accessioned2026-07-07T03:09:37Z
dc.date.available2026-07-07T03:09:37Z
dc.descriptionA two amino acid (hydrophobic and polar) scheme is used to perform the design on target conformations corresponding to the native states of twenty single chain proteins. Strikingly, the percentage of successful identification of the nature of the residues benchmarked against naturally occurring proteins and their homologues is around 75 % independent of the complexity of the design procedure. Typically, the lowest success rate occurs for residues such as alanine that have a high secondary structure functionality. Using a simple lattice model, we argue that one possible shortcoming of the model studied may involve the coarse-graining of the twenty kinds of amino acids into just two effective types.
dc.description14 pages, 9 colour figures
dc.identifierhttps://arxiv.org/abs/cond-mat/9712124
dc.identifierhttp://arxiv.org/abs/cond-mat/9712124
dc.identifier.urihttp://salesiana.dossiersoluciones.com/handle/123456789/27956
dc.subjectStatistical Mechanics
dc.subjectSoft Condensed Matter
dc.subjectBiomolecules
dc.titleInverse design of proteins with hydrophobic and polar amino acids
dc.typetext

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