Folding simulations of the A and B domains of protein G.
We study wild type and mutants of the A and B domain of protein G using all-atom Go-models. Our data substantiate the usefulness of such simulation for probing the folding mechanism of proteins and demonstrate that multifunnel versions of such models also allow probing of more complicated funnel landscapes. In our case, such models reproduce the experimentally observed distributions of the GA98 and GB98 mutants which differ only by one residue but fold into different structures. They also reveal details on the folding mechanism in these two proteins.
Department of Physics, Michigan Technological University, Houghton, Michigan 49931, USA. mkouza@mtu.edu
Maksim
M
Kouza
Ulrich H E
UH
Hansmann
D019206:GTP-Binding Protein alpha Subunits, Gi-Go / Q000737:chemistry* / Q000235:genetics; D008958:Models, Molecular; D056004:Molecular Dynamics Simulation; D017510:Protein Folding
D019206:GTP-Binding Protein alpha Subunits, Gi-Go