Arginine and Lysine interactions with ? residues in metalloproteins.
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ABSTRACT:
SUBMITTER: Anitha P
PROVIDER: S-EPMC3488845 | biostudies-literature | 2012
REPOSITORIES: biostudies-literature
Publications
Arginine and Lysine interactions with π residues in metalloproteins.
Anitha Parimelzaghan P Sivasakthi Vaideeswaran V Lavanya Pandian P Bag Susmita S Kumar Kalavathi Murugan KM Anbarasu Anand A Ramaiah Sudha S
Bioinformation 20120911 17
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 metal ...[more]
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