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Explanation of the stability of thermophilic proteins based on unique micromorphology (Articolo in rivista)
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- Label
- Explanation of the stability of thermophilic proteins based on unique micromorphology (Articolo in rivista) (literal)
- Anno
- 2006-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1529/biophysj.105.078972 (literal)
- Alternative label
Melchionna, S; Sinibaldi, R; Briganti, G (2006)
Explanation of the stability of thermophilic proteins based on unique micromorphology
in Biophysical journal (Print)
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Melchionna, S; Sinibaldi, R; Briganti, G (literal)
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- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
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- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- Univ Roma La Sapienza, Dept Phys, SOFT, Ist Nazl Fis Mat, I-00161 Rome, Italy; Univ Politecn Marche, Dipartimento Sci Applicate Sist Complessi, Ancona, Italy (literal)
- Titolo
- Explanation of the stability of thermophilic proteins based on unique micromorphology (literal)
- Abstract
- Two mesophilic/thermophilic variants of the G-domain of the elongation factor Tu were studied via molecular dynamics simulations. By analyzing the simulation data via the Voronoi space tessellation, we have found that the two proteins have the same macromolecular packing, while the water-exposed surface area is larger for the thermophile. A larger coordination with water is probably due to a peculiar corrugation of the exposed surface of this species. From an enthalpic point of view, the thermophile shows a larger number of intramolecular hydrogen bonds, stronger electrostatic interactions, and a flatter free-energy landscape. Overall, the data suggest that the specific hydration state enhances macromolecular fluctuations but, at the same time, increases thermal stability. (literal)
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