caa a22 4500 605507368 CHVBK 20210128100631.0 cr unu---uuuuu 210128e20150401xx s 000 0 eng 10.1007/s00775-014-1235-1 doi (NATIONALLICENCE)springer-10.1007/s00775-014-1235-1 Interaction between dimer interface residues of native and mutated SOD1 protein: a theoretical study [Elektronische Daten] [S. Keerthana, P. Kolandaivel] Cu-Zn superoxide dismutase 1 (SOD1) is a highly conserved bimetallic protein enzyme, used for the scavenging the superoxide radicals (O2 −) produced due to aerobic metabolism in the mitochondrial respiratory chain. Over 100 mutations have been identified and found to be in the homodimeric structure of SOD1. The enzyme has to be maintained in its dimeric state for the structural stability and enzymatic activity. From our investigation, we found that the mutations apart from the dimer interface residues are found to affect the dimer stability of protein and hence enhancing the aggregation and misfolding tendency of mutated protein. The homodimeric state of SOD1 is found to be held together by the non-covalent interactions. The molecular dynamics simulation has been used to study the hydrogen bond interactions between the dimer interface residues of the monomers in native and mutated forms of SOD1 in apo- and holo-states. The results obtained by this analysis reveal the fact that the loss of hydrogen bond interactions between the monomers of the dimer is responsible for the reduced stability of the apo- and holo-mutant forms of SOD1. The conformers with dimer interface residues in native and mutated protein obtained by the molecular dynamics simulation is subjected to quantum mechanical study using M052X/6-31G(d) level of theory. The charge transfer between N-H···O interactions in the dimer interface residues were studied. The weak interaction between the monomers of the dimer accounts for the reduced dimerization and enhanced deformation energy in the mutated SOD1 protein. SBIC, 2015 Superoxide radicals nationallicence Dimer interface residues nationallicence Molecular dynamics nationallicence Hydrogen bond interactions nationallicence Keerthana S. Department of Physics, Bharathiar University, 641 046, Coimbatore, India aut Kolandaivel P. Department of Physics, Bharathiar University, 641 046, Coimbatore, India aut JBIC Journal of Biological Inorganic Chemistry Springer Berlin Heidelberg 20/3(2015-04-01), 509-522 0949-8257 20:3<509 2015 20 775 https://doi.org/10.1007/s00775-014-1235-1 text/html Onlinezugriff via DOI BK010053 XK010053 XK010000 Metadata rights reserved Springer special CC-BY-NC licence nationallicence 1 research-article jats NATIONALLICENCE NATIONALLICENCE NL-springer NATIONALLICENCE 856 40 https://doi.org/10.1007/s00775-014-1235-1 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Keerthana S. Department of Physics, Bharathiar University, 641 046, Coimbatore, India aut NATIONALLICENCE 700 1- Kolandaivel P. Department of Physics, Bharathiar University, 641 046, Coimbatore, India aut NATIONALLICENCE 773 0- JBIC Journal of Biological Inorganic Chemistry Springer Berlin Heidelberg 20/3(2015-04-01), 509-522 0949-8257 20:3<509 2015 20 775