Elucidating the protein cold-adaptation: Investigation of the parameters enhancing protein psychrophilicity.
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.
Jahandideh
Mina
M
Department of Mathematics, Faculty of Science, Vali-E-Asr University, Rafsanjan, Iran.
Barkooie
Seyyed Mohsen Hosseini
SM
Jahandideh
Samad
S
Abdolmaleki
Parviz
P
Movahedi
Mohammad Mehdi
MM
Hoseini
Somayyeh
S
Asadabadi
Ebrahim Barzegari
EB
Jouni
Fatemeh Javani
FJ
Karami
Zahra
Z
Firoozabadi
Nader Hodjati
NH
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
D021301:Antifreeze Proteins