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Protein & Peptide Letters
ISSN (Print): 0929-8665
ISSN (Online): 1875-5305
Epub Abstract Ahead of Print
DOI: 10.2174/0929866521666140108110050      Price:  $95

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

Author(s): Zhaolin Mou, Yanrui Ding, Xueqin Wang and Yujie Cai
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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
Key Laboratory of Advanced Process Control for Light Industry, Jiangnan University, Wuxi, Jiangsu PR, China