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.
journal_name
Biophys Jjournal_title
Biophysical journalauthors
Melchionna S,Sinibaldi R,Briganti Gdoi
10.1529/biophysj.105.078972subject
Has Abstractpub_date
2006-06-01 00:00:00pages
4204-12issue
11eissn
0006-3495issn
1542-0086pii
S0006-3495(06)72599-1journal_volume
90pub_type
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