Ontology highlight
ABSTRACT:
SUBMITTER: Spadaccini R
PROVIDER: S-EPMC7164040 | biostudies-literature | 2014 Feb
REPOSITORIES: biostudies-literature
Spadaccini Roberta R Ercole Carmine C Graziano Giuseppe G Wechselberger Rainer R Boelens Rolf R Picone Delia D
The FEBS journal 20140201 3
3D domain swapping (3D-DS) is a complex protein aggregation process for which no unique mechanism exists. We report an analysis of 3D-DS in bovine seminal ribonuclease, a homodimeric protein whose subunits are linked by two disulfide bridges, based on NMR and biochemical studies. The presence of the covalent bonds between the subunits stabilizes the unswapped dimer, and allows distinct evaluation of the structural and dynamic effects of the swapping with respect to the dimerization process. In c ...[more]