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.
Highlights
Metalloproteins are the most extensively studied class of biomacromolecules in the field of biological inorganic chemistry [1] and in environment protection [2]
The higher number of energetically significant cation-π interactions with Trp residues in spite of its lower occurrence in metalloproteins is an important observation in the present study and Trp residues might play an important role in the structural stability of metalloproteins through Arg/Lys interactions with π residues
In terms of energetically significant Arg/Lys interactions with π residues in the study group, the energies from Arg interactions are higher when compared with Lys interactions with π residues
Summary
Metalloproteins are the most extensively studied class of biomacromolecules in the field of biological inorganic chemistry [1] and in environment protection [2]. In the field of protein design and engineering, metalloproteins make attractive targets [3]. There are many reasons for this, including the exciting possibility of engineering protein-based molecules with useful catalytic, electronic or optoelectronic properties. Another important reason for their popularity as targets is that metal binding makes available plenty of energy, which helps to compensate for the deficiencies in our ability to design sequences that fold into well-packed, stable structures. Metalbinding sites have been built into existing protein scaffolds or into scaffolds that have been designed de novo, usually with computational screening of structures for appropriate ligand positions [4]
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
