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Protein & Peptide Letters

Editor-in-Chief

ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

Comparison of Protein-water Interactions in Psychrophilic, Mesophilic, and Thermophilic Fe-SOD

Author(s): Zhaolin Mou, Yanrui Ding, Xueqin Wang and Yujie Cai

Volume 21, Issue 6, 2014

Page: [578 - 583] Pages: 6

DOI: 10.2174/0929866521666140108110050

Price: $65

Abstract

Iron superoxide dismutase (Fe-SOD) can eliminate superoxide anion radicals and is widely used in pharmaceuticals, cosmetics and foodstuff. It’s significant to determine the factors that influence Fe-SOD thermostability. Previous studies have focused on the relationship between the structural parameters and thermostability of Fe-SOD while the contribution of water molecules was overlooked. In this study, we examined the relationship between hydration waters and Fe-SOD thermostability. The Voronoi polyhedra method was used to explore the distribution of hydration waters around the Fe-SODs and it was interesting to find that the distribution of hydration waters is related to the B-factor of amino acids, i.e., the flexibility of residues can affect the distribution of waters. Protein-water and water-water hydrogen bonds were examined. We found that the hydrogen bond density in thermophilic Fe-SOD was higher than that in mesophilic Fe- SOD. In addition, larger hydrogen bond networks that involve more waters covered the thermophilic Fe-SOD.

Keywords: Hydration waters, hydrogen bond network, iron superoxide dismutase, protein thermostability, temperature factor, Voronoi polyhedra.


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