Ontology highlight
ABSTRACT:
SUBMITTER: Suresh A
PROVIDER: S-EPMC2859576 | biostudies-literature | 2009 Nov
REPOSITORIES: biostudies-literature
Suresh Abishek A Karthikraja Velmurugan V Lulu Sajitha S Kangueane Uma U Kangueane Pandjassarame P
Bioinformation 20091117 5
The formation of protein homodimer complexes for molecular catalysis and regulation is fascinating. The homodimer formation through 2S (2 state), 3SMI (3 state with monomer intermediate) and 3SDI (3 state with dimer intermediate) folding mechanism is known for 47 homodimer structures. Our dataset of forty-seven homodimers consists of twenty-eight 2S, twelve 3SMI and seven 3SDI. The dataset is characterized using monomer length, interface area and interface/total (I/T) residue ratio. It is found ...[more]