title: Arginine and Lysine interactions with π residues in metalloproteins.
abstract: Metalloproteins have many different functions in cells such as enzymes; signal transduction, transport and storage proteins. About one third of all proteins require metals to carry out their functions. In the present study we have analyzed the roles played by Arg and Lys (cationic side chains) interactions with π (Phe, Tyr or Trp) residues and their role in the structural stability of metalloproteins. These interactions might play an important role in the global conformational stability in metalloproteins. In spite of its lower natural occurrence (1.76%) the number of Trp residues involved in energetically significant interactions is higher in metalloproteins.
authors.affiliation: Bioinformatics Division, School of Biosciences & Technology, VIT University, Vellore-632014, India.
authors.forename: Parimelzaghan
authors.initials: P
authors.lastname: Anitha
authors.forename: Vaideeswaran
authors.initials: V
authors.lastname: Sivasakthi
authors.forename: Pandian
authors.initials: P
authors.lastname: Lavanya
authors.forename: Susmita
authors.initials: S
authors.lastname: Bag
authors.forename: Kalavathi Murugan
authors.initials: KM
authors.lastname: Kumar
authors.forename: Anand
authors.initials: A
authors.lastname: Anbarasu
authors.forename: Sudha
authors.initials: S
authors.lastname: Ramaiah
keywords: Arginine; Lysine; Metalloproteins; sequential distance; π interactions