The Designability of Protein Structures: A Lattice-Model Study using the Miyazawa-Jernigan Matrix

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dc.creatorLi, Hao
dc.creatorTang, Chao
dc.creatorWingreen, Ned
dc.date2002-03-22
dc.date.accessioned2026-07-07T02:44:47Z
dc.date.available2026-07-07T02:44:47Z
dc.descriptionWe study the designability of all compact 3x3x3 and 6x6 lattice-protein structures using the Miyazawa-Jernigan (MJ) matrix. The designability of a structure is the number of sequences that design the structure, i.e. sequences that have that structure as their unique lowest-energy state. Previous studies of hydrophobic-polar (HP) models showed a wide distribution of structure designabilities. Recently, questions were raised concerning the use of a 2-letter (HP) code in such studies. Here we calculate designabilities using all 20 amino acids, with empirically determined interaction potentials (MJ matrix), and compare with HP model results. We find good qualitative agreement between the two models. In particular, highly designable structures in the HP model are also highly designable in the MJ model--and vice versa--with the associated sequences having enhanced thermodynamic stability.
dc.description32 pages, 13 figures
dc.identifierhttps://arxiv.org/abs/cond-mat/0203481
dc.identifierhttp://arxiv.org/abs/cond-mat/0203481
dc.identifierProteins 49, 403 (2002).
dc.identifier.urihttp://salesiana.dossiersoluciones.com/handle/123456789/19071
dc.subjectStatistical Mechanics
dc.subjectSoft Condensed Matter
dc.subjectBiomolecules
dc.titleThe Designability of Protein Structures: A Lattice-Model Study using the Miyazawa-Jernigan Matrix
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