title: Shedding light on the extra thermal stability of thermophilic proteins.
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.
authors.affiliation: Dipartimento di Scienze Chimiche, Università degli Studi di Napoli Federico II, Complesso Universitario di Monte Sant'Angelo, Via Cintia, Napoli, 80126, Italy.
authors.forename: Andrea
authors.initials: A
authors.lastname: Pica
authors.affiliation: Dipartimento di Scienze e Tecnologie, Università del Sannio, Via Port'Arsa 11, Benevento, 82100, Italy. graziano@unisannio.it.
authors.forename: Giuseppe
authors.initials: G
authors.lastname: Graziano
mesh_terms: D000818:Animals; D003080:Cold Temperature; D019277:Entropy; D006358:Hot Temperature; D006801:Humans; D008956:Models, Chemical; D011489:Protein Denaturation; D055550:Protein Stability; D011506:Proteins / Q000737:chemistry*
chemical_list: D011506:Proteins
keywords: conformational entropy; geometric model; solvent-excluded volume effect; thermophilic proteins