Sequence and Structural Parameters Enhancing Adaptation of Proteins to Low Temperatures.
From: Department of Biophysics, Faculty of Science, Tarbiat Modares University, Tehran, Iran.
Journal of theoretical biology
- Publish Date: May 2007
- ISSN: 0022-5193
- Volume: 246
- Issue: 1
- Pages: 159-66
- Medium: Print
- Language: English
- Citation (JAMA): Jahandideh Samad, Abdolmaleki Parviz, Jahandideh Mina, et al. Sequence and Structural Parameters Enhancing Adaptation of Proteins to Low Temperatures.. J. Theor. Biol. May 2007;246:159-66
Abstract
A systematic analysis compared sequence and structural parameters distributions between 13 pairs of psychrophilic and mesophilic proteins for elucidating the cold adaptation parameters. The results of statistical test (t-test) revealed that helical content, tight turn content, disulfide bonds and hydrogen bonds do not show significant difference between psychrophilic and mesophilic proteins. However, it was demonstrated in this study that a larger proportion of open beta-turn in psychrophilic proteins is an effective parameter in specific activity at low temperature. In addition, substitution of amino acids of charged and aliphatic groups with amino acids of tiny and small groups in protein chains, tight turns and alpha-helices in the direction from mesophilic to psychrophilic proteins is one of the mechanisms of low temperature adaptation. Such sequence and structural parameter differences would help to develop a strategy for designing cold-adapted proteins.
Mesh Headings (Keywords): Adaptation, Physiological, Amino Acid Sequence, Animals, Cold, Hydrogen Bonding, Models, Molecular, Molecular Sequence Data, Protein Conformation, Protein Structure, Secondary, Proteins
Check for Full Text / PubMed Unique Identifier (PMID): 17275036
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