Measuring Intrinsic Disorder and Tracking Conformational Transitions Using Rosetta ResidueDisorder.

ABSTRACT: Many proteins contain regions of intrinsic disorder, not folding into unique, stable conformations. Numerous experimental methods have been developed to measure the disorder of all or select residues. In the absence of experimental data, computational methods are often utilized to identify these disordered regions and thus gain a better understanding of both structure and function. Many freely available computational methods have been developed to predict regions of intrinsic disorder from the primary sequence of a protein, including our recently developed Rosetta ResidueDisorder. While these methods are very useful, they are only designed to predict intrinsic disorder from the sequence. However, it would be useful to have a method that could also measure intrinsic disorder directly from s

SUBMITTER: Seffernick JT 

PROVIDER: S-EPMC6748046 | biostudies-literature | 2019 Aug

REPOSITORIES: biostudies-literature