A critical evaluation of in silico methods for detection of membrane protein intrinsic disorder.

ABSTRACT: Intrinsically disordered regions in proteins possess important biological roles including transcriptional regulation, molecular recognition, and provision of sites for posttranslational modification. In three-dimensional crystallization of both soluble and membrane proteins, identification and removal of disordered regions is often necessary for obtaining crystals possessing sufficient long-range order for structure determination. Disordered regions can be identified experimentally, with techniques such as limited proteolysis coupled with mass spectrometry, or computationally, by using disorder prediction programs, of which many are available. Although these programs use various methods to predict disorder from a protein's primary sequence, they all were developed using information derived

SUBMITTER: Pryor EE 

PROVIDER: S-EPMC4008797 | biostudies-literature | 2014 Apr

REPOSITORIES: biostudies-literature