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Physicochemical Properties of Insect and Plant Antifreeze Proteins:A Computational Study


Affiliations
1 Centre for Nanotechnology and Advanced Biomaterials, SASTRA University, Thirumalaisamudram, Thanjavur 613 401, India
 

Antifreeze proteins are found in cold-surviving organisms. These proteins have greater structural diversity among same and different species. In this study, a total of 14 antifreeze proteins from both insects and plants were selected randomly and their physicochemical characteristics along with their structural features were analysed using computational tools. The results indicate that plant antifreeze proteins are mostly hydrophilic, which can interact with ice/water effectively. The study shows that the thermal stability of plant antifreeze proteins is greater than insect antifreeze proteins. Among the chosen sequences, insect antifreeze proteins were mostly β-sheet and plant antifreeze proteins were α-helix.

Keywords

Antifreeze Proteins, Disulphide Bonds, Homology Modelling, Hydrophobicity, Thermal Stability.
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  • Physicochemical Properties of Insect and Plant Antifreeze Proteins:A Computational Study

Abstract Views: 191  |  PDF Views: 74

Authors

L. Ramya
Centre for Nanotechnology and Advanced Biomaterials, SASTRA University, Thirumalaisamudram, Thanjavur 613 401, India

Abstract


Antifreeze proteins are found in cold-surviving organisms. These proteins have greater structural diversity among same and different species. In this study, a total of 14 antifreeze proteins from both insects and plants were selected randomly and their physicochemical characteristics along with their structural features were analysed using computational tools. The results indicate that plant antifreeze proteins are mostly hydrophilic, which can interact with ice/water effectively. The study shows that the thermal stability of plant antifreeze proteins is greater than insect antifreeze proteins. Among the chosen sequences, insect antifreeze proteins were mostly β-sheet and plant antifreeze proteins were α-helix.

Keywords


Antifreeze Proteins, Disulphide Bonds, Homology Modelling, Hydrophobicity, Thermal Stability.

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DOI: https://doi.org/10.18520/cs%2Fv112%2Fi07%2F1512-1520