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Application of principal component analysis to determine the key structural features contributing to iron superoxide dismutase thermostability
Author(s) -
Ding Yanrui,
Cai Yujie,
Han Yonggang,
Zhao Bingqiang,
Zhu Lei
Publication year - 2012
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.22093
Subject(s) - thermostability , chemistry , superoxide dismutase , hydrogen bond , crystallography , thermal stability , salt bridge , helix (gastropod) , enzyme , biochemistry , molecule , organic chemistry , ecology , biology , snail , mutant , gene
Iron superoxide dismutase (Fe‐SOD) is predominantly found in bacteria and mitochondria. The thermal stability of Fe‐SOD from different sources can vary dramatically. We have studied the influence of structural parameters on Fe‐SOD thermostability by principal component analysis (PCA). The results show that an increased α‐helical and turn content, an increased α‐helix and loop length, an increase in the number of main‐main chains and charged‐uncharged hydrogen bonds, a decrease in the 3 10 ‐helix content, and a decreased β‐strand and loop length are all important factors for Fe‐SOD thermostability. Interestingly, the use of charged residues to form salt bridges is tendentious in thermophilic Fe‐SOD. Negatively charged Arg and positively charged Glu are efficiently used to form salt bridges. The cooperative action of the exposed area, the hydrogen bonds, and the secondary structure plays a crucial role in resisting high temperatures, which demonstrates that the increased stability of thermophilic Fe‐SOD is provided by several structural factors acting together. © 2012 Wiley Periodicals, Inc. Biopolymers 97:864–872, 2012.