caa a22 4500 445840536 CHVBK 20180317145342.0 cr unu---uuuuu 170323e20111001xx s 000 0 eng 10.1007/s00709-010-0224-7 doi (NATIONALLICENCE)springer-10.1007/s00709-010-0224-7 Structural stability studies in adhesion molecules—role of cation- π interactions [Elektronische Daten] [K. Sophiya, Anand Anbarasu] 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. Springer-Verlag, 2010 Adhesion molecules nationallicence Cation- π interactions nationallicence Secondary structure nationallicence Conservation patterns nationallicence Stabilization centers nationallicence CAM : Cell adhesion molecule nationallicence ECM : Extracellular matrix nationallicence Arg (R) : Arginine nationallicence Lys (K) : Lysine nationallicence Phe (F) : Phenyl alanine nationallicence Tyr (Y) : Tyrosine nationallicence Trp (W) : Tryptophan nationallicence DSSP : Dictionary of protein secondary structure nationallicence E es : Electrostatic energy nationallicence E vdw : Van der Waals energy nationallicence E cat- π : Total cation-π interaction energy nationallicence PDB : Protein data bank nationallicence CAPTURE : Cation Pi Trends Using Realistic Electrostatics nationallicence Sophiya K. Bioinformatics Division, School of Biosciences & Technology, VIT University, 632014, Vellore, India aut Anbarasu Anand Bioinformatics Division, School of Biosciences & Technology, VIT University, 632014, Vellore, India aut Protoplasma Springer Vienna 248/4(2011-10-01), 673-682 0033-183X 248:4<673 2011 248 709 https://doi.org/10.1007/s00709-010-0224-7 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s00709-010-0224-7 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Sophiya K. Bioinformatics Division, School of Biosciences & Technology, VIT University, 632014, Vellore, India aut NATIONALLICENCE 700 1- Anbarasu Anand Bioinformatics Division, School of Biosciences & Technology, VIT University, 632014, Vellore, India aut NATIONALLICENCE 773 0- Protoplasma Springer Vienna 248/4(2011-10-01), 673-682 0033-183X 248:4<673 2011 248 709 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer