title: Elucidating the protein cold-adaptation: Investigation of the parameters enhancing protein psychrophilicity.
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.
authors: Department of Mathematics, Faculty of Science, Vali-E-Asr University, Rafsanjan, Iran.
authors: Mina
authors: M
authors: Jahandideh
authors: Seyyed Mohsen Hosseini
authors: SM
authors: Barkooie
authors: Samad
authors: S
authors: Jahandideh
authors: Parviz
authors: P
authors: Abdolmaleki
authors: Mohammad Mehdi
authors: MM
authors: Movahedi
authors: Somayyeh
authors: S
authors: Hoseini
authors: Ebrahim Barzegari
authors: EB
authors: Asadabadi
authors: Fatemeh Javani
authors: FJ
authors: Jouni
authors: Zahra
authors: Z
authors: Karami
authors: Nader Hodjati
authors: NH
authors: Firoozabadi
mesh_terms: D000222:Adaptation, Physiological; D019943:Amino Acid Substitution; D000818:Animals; D021301:Antifreeze Proteins / Q000737:chemistry*; D003080:Cold Temperature; D030562:Databases, Protein; D008956:Models, Chemical; D017433:Protein Structure, Secondary; D013329:Structure-Activity Relationship
chemical_list: D021301:Antifreeze Proteins