Structural stability studies in adhesion molecules--role of cation-π interactions.
Cell adhesion molecules are important for their various roles in many cellular events and responses. In the present study, we have analyzed the roles played by cation-π interactions in the structural stability of adhesion molecules. These interactions are mainly formed by long-range contacts. The occurrence of arginine is higher than lysine to form cation-π interactions. The secondary structure preferences of interacting residues are independent of amino acid class. Cation-π interactions might stabilize the interface between the terminus and core in this class of proteins. The results obtained in the present study will be useful in understanding the contribution of cation-π interactions to the overall stability of adhesion proteins.
Bioinformatics Division, School of Biosciences & Technology, VIT University, Vellore, 632014, India.
K
K
Sophiya
Anand
A
Anbarasu
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000737:chemistry; D002412:Cations / Q000737:chemistry*; D015815:Cell Adhesion Molecules / Q000737:chemistry*; D019295:Computational Biology; D017124:Conserved Sequence; D030562:Databases, Protein; D025941:Protein Interaction Mapping; D055550:Protein Stability; D017433:Protein Structure, Secondary; D016415:Sequence Alignment; D020539:Sequence Analysis, Protein; D012997:Solvents / Q000737:chemistry
D000596:Amino Acids; D002412:Cations; D015815:Cell Adhesion Molecules; D012997:Solvents