title: Predicting properties of intrinsically unstructured proteins.
abstract: There is increasing evidence that intrinsically unstructured proteins or protein domains have important biological functions. These types of proteins may be productively analyzed using polymer theory developed to predict global physical properties of polymers. In these theories molecular detail is "coarse grained" out of the models, and replaced with a small number of parameters that characterize the polymer. This reduction in complexity allows extremely large systems to be studied. In the case of simulations, the time scales accessible also increase significantly. Here we discuss the application of polymer theory to unstructured proteins, and consider how to classify proteins within a polymer framework. We then review polymer theory that is relevant to predicting functionally important properties, such as radius of gyration, height of a polymer brush and force required to compress a polymer brush.
authors.affiliation: Department of Physiology, School of Medicine, Johns Hopkins University, 725 N. Wolfe Street, Baltimore, MD 21205, USA.
authors.forename: J N
authors.initials: JN
authors.lastname: Bright
authors.forename: T B
authors.initials: TB
authors.lastname: Woolf
authors.forename: J H
authors.initials: JH
authors.lastname: Hoh
mesh_terms: D001704:Biopolymers / Q000145:classification; D004563:Electrochemistry; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry* / Q000502:physiology*; D013499:Surface Properties
chemical_list: D001704:Biopolymers; D011506:Proteins