The role of cofactors, like transition metal ions, in folding, misfolding and aggregating proteins and peptides within cells and tissues is now well recognized [1]. Due to the low degree of structure in protein regions involved in such important interactions, experimental methods need complementary information provided by models, these latter ranging from coarse-grained electrostatics to accurate quantum-mechanical descriptions of forces, passing through empirical force-fields used in atomistic simulations. In this contribution, the role of different types of modeling techniques and of high-performance computing infrastructures will be described, with particular emphasis on the contributions provided to the understanding of the interactions between Zn/Cu and peptides involved in neurodegenerative disorders like Creutzfeldt-Jacob (prion protein) [2,3] and Alzheimer's diseases (amyloid-beta peptides) [4,5,6].
Modeling interactions between peptides and metal ions
La Penna;Giovanni
2012
Abstract
The role of cofactors, like transition metal ions, in folding, misfolding and aggregating proteins and peptides within cells and tissues is now well recognized [1]. Due to the low degree of structure in protein regions involved in such important interactions, experimental methods need complementary information provided by models, these latter ranging from coarse-grained electrostatics to accurate quantum-mechanical descriptions of forces, passing through empirical force-fields used in atomistic simulations. In this contribution, the role of different types of modeling techniques and of high-performance computing infrastructures will be described, with particular emphasis on the contributions provided to the understanding of the interactions between Zn/Cu and peptides involved in neurodegenerative disorders like Creutzfeldt-Jacob (prion protein) [2,3] and Alzheimer's diseases (amyloid-beta peptides) [4,5,6].I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
