|
|||||
|
|
Predicting properties of intrinsically unstructured proteins |
|
| Authors: | Joanne N. Bright Thomas B. Woolf Jan H. Hoh |
| Affiliation: | a Department of Physiology, School of Medicine, Johns Hopkins University, 725 N. Wolfe Street, Baltimore, MD 21205, USA b Department of Biophysics, School of Medicine, Johns Hopkins University, 725 N. Wolfe Street, Baltimore, MD 21205, USA c Department of Biomedical Engineering, School of Medicine, Johns Hopkins University, 725 N. Wolfe Street, Baltimore, MD 21205, USA d Department of Chemical Engineering, Johns Hopkins University, Baltimore, MD 21218, USA |
| 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. |
| Keywords: | Polymer theory Protein structure |
| 本文献已被 ScienceDirect 等数据库收录！ | |