Design of Proteins with Specified Thermal Properties

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dc.creatorMorrissey, Michael P.
dc.creatorShakhnovich, Eugene I.
dc.date1996-01-25
dc.date.accessioned2026-07-07T03:08:10Z
dc.date.available2026-07-07T03:08:10Z
dc.descriptionWe propose a new and effective means for designing stable and fast-folding polypeptide sequences using a cumulant expansion of the molecular partition function. This method is unique in that $T_{Z}$, the ``cumulant design temperature'' entered as a parameter in the design process, is predicted also to be the optimal folding temperature. The method was tested using monte-carlo folding simulations of the designed sequences, at various folding temperatures $T_{F}$. (Folding simulations were run on a cubic lattice for computational convenience, but the design process itself is lattice-independent.) Simulations confirmed that, over a wide range of $T_{Z}$, all designed sequences folded rapidly when $T_{F} \approx T_{Z}$. Additionally, highly thermostable model proteins were created simply by designing with high $T_{Z}$. The mechanism proposed in these studies provides a plausible pathway for the evolutionary design of biologically active proteins, which {\em must} fold and remain stable within a relatively narrow range of temperatures.
dc.description12 pages (RevTeX) + 4 postscript figures
dc.identifierhttps://arxiv.org/abs/cond-mat/9601120
dc.identifierhttp://arxiv.org/abs/cond-mat/9601120
dc.identifier.urihttp://salesiana.dossiersoluciones.com/handle/123456789/27450
dc.subjectCondensed Matter
dc.subjectQuantitative Biology
dc.titleDesign of Proteins with Specified Thermal Properties
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