The Relation among Thermodynamic Stability, Folding Dynamics, and Designability
نویسندگان
چکیده
منابع مشابه
Designability , thermodynamic stability , and
In the framework of a lattice-model study of protein folding, we investigate the interplay between designability, thermodynamic stability, and kinetics. To be \protein-like", heteropolymers must be thermodynamically stable, stable against mutating the amino-acid sequence, and must be fast folders. We nd two criteria which, together, guarantee that a sequence will be \protein like": i) the groun...
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In the framework of a lattice-model study of protein folding, we investigate the interplay between designability, thermodynamic stability, and kinetics. To be ‘‘protein-like,’’ heteropolymers must be thermodynamically stable, stable against mutating the amino-acid sequence, and must be fast folders. We find two criteria which, together, guarantee that a sequence will be ‘‘protein like:’’ ~i! th...
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It is well-known that the typical protein’s three-dimensional structure is relatively unstable in harsh conditions. A practical approach to maintain the folded state and thus improve the stability and activity of proteins in unusual circumstances is to directly apply stabilizing substances such as osmolytes to the protein-containing solutions. Osmolytes as natural occurring organic molecules ty...
متن کاملOsmolyte-Induced Folding and Stability of Proteins: Concepts and Characterization
It is well-known that the typical protein’s three-dimensional structure is relatively unstable in harsh conditions. A practical approach to maintain the folded state and thus improve the stability and activity of proteins in unusual circumstances is to directly apply stabilizing substances such as osmolytes to the protein-containing solutions. Osmolytes as natural occurring organic molecules ty...
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ژورنال
عنوان ژورنال: Progress of Theoretical Physics Supplement
سال: 2000
ISSN: 0375-9687
DOI: 10.1143/ptps.138.420