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Elucidating the protein cold-adaptation: Investigation of the parameters enhancing protein psychrophilicity
Authors:Jahandideh Mina  Barkooie Seyyed Mohsen Hosseini  Jahandideh Samad  Abdolmaleki Parviz  Movahedi Mohammad Mehdi  Hoseini Somayyeh  Asadabadi Ebrahim Barzegari  Jouni Fatemeh Javani  Karami Zahra  Firoozabadi Nader Hodjati
Institution:a Department of Mathematics, Faculty of Science, Vali-E-Asr University, Rafsanjan, Iran
b Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran
c Department of Biophysics, Faculty of Science, Tarbiat Modares University, P.O. Box 14115/175, Tehran, Iran
d Department of Medical Physics, Shiraz University of Medical Sciences, Shiraz, Iran
e Department of Genetics, Division of Biochemistry, Tabriz University of Medical Sciences, Tabriz, Iran
f Sina Trauma Research Center, Sina General Hospital, Tehran University of Medical Sciences, Tehran, Iran
Abstract:To investigate the role of the critical parameters in adaptation of proteins to low temperatures, a comparative systematic analysis was performed. Several parameters were proposed to have contribution to cold adaptation of proteins. Among proposed parameters, total values of residual structure states, secondary structure states and oligomeric states were alike in both psychrophilic and mesophilic proteins. In addition, our results provided new quantitative information about the trends in the substitution preference of Ile, Phe, Tyr, Lys, Arg, His, Glu and Leu with most of amino acids and substitution avoidance of Gly, Thr and Ala with most of amino acids. These findings would help future efforts propose a strategy for designing psychrophilic proteins.
Keywords:Psychrophilic protein  Structural analysis  Substitution preference  Systematic analysis
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