Shedding light on the extra thermal stability of thermophilic proteins |
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Authors: | Andrea Pica Giuseppe Graziano |
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Affiliation: | 1. Dipartimento di Scienze Chimiche, Università degli Studi di Napoli Federico II, Complesso Universitario di Monte Sant'Angelo, Napoli, Italy;2. Dipartimento di Scienze e Tecnologie, Università del Sannio, Benevento, Italy |
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Abstract: | An entropic stabilization mechanism has recently gained attention and credibility as the physical ground for the extra thermal stability of globular proteins from thermophilic microorganisms. An empirical result, obtained from the analysis of thermodynamic data for a large set of proteins, strengthens the general reliability of the theoretical approach originally devised to rationalize the occurrence of cold denaturation [Graziano, PCCP 2014, 16, 21755–21767]. It is shown that this theoretical approach can readily account for the entropic stabilization mechanism. On decreasing the conformational entropy gain associated with denaturation, the thermal stability of a model globular protein increases markedly. |
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Keywords: | conformational entropy geometric model solvent‐excluded volume effect thermophilic proteins |
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