Folding and unfolding for binding: large-scale protein dynamics in protein-protein interactions.
The role of dynamics in the function of proteins, from enzymes to signalling proteins, is widely recognized. In many cases, the dynamic process is a relatively localized one, involving motion of a limited number of key residues, while in others large-scale domain movements may be involved. These motions all take place within the context of a folded protein; however, there is increasing evidence for the existence of some proteins where a transition between folded and unfolded structures is required for function.
Roberts
G C K
GC
Henry Wellcome Laboratories for Structural Biology, Department of Biochemistry, Henry Wellcome Building, University of Leicester, P.O. Box 138, Lancaster Road, Leicester LE1 9HN, UK. gcr@le.ac.uk
D007700:Kinetics; D008958:Models, Molecular; D011485:Protein Binding; D011487:Protein Conformation; D011489:Protein Denaturation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism*; D016608:Talin / Q000737:chemistry / Q000378:metabolism
D011506:Proteins; D016608:Talin