Determination of conformationally heterogeneous states of proteins.
Although conformationally heterogeneous states of proteins are involved in a range of important biological processes, including protein folding and misfolding, and signal transduction, detailed knowledge of their structure and dynamics is still largely missing. Proteins in many of these states are constantly changing shape, such that they are better described as ensembles of conformations rather than in terms of well-defined structures, as is normally the case for native states. Methods in which molecular simulations are combined with experimental measurements are emerging as a powerful route to the accurate determination of the conformational properties of these states of proteins.
Vendruscolo
Michele
M
Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK. mv245@cam.ac.uk
D019295:Computational Biology / Q000379:methods; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D011487:Protein Conformation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*; D015203:Reproducibility of Results
D011506:Proteins