Prediction of intrinsic disorder and its use in functional proteomics.

38Citations
Citations of this article
23Readers
Mendeley users who have this article in their library.
Get full text

Abstract

The number of experimentally verified, intrinsically disordered (ID) proteins is rapidly rising. Research is often focused on a structural characterization of a given protein, looking for several key features. However, ID proteins with their dynamic structures that interconvert on a number of time-scales are difficult targets for the majority of traditional biophysical and biochemical techniques. Structural and functional analyses of these proteins can be significantly aided by disorder predictions. The current advances in the prediction of ID proteins and the use of protein disorder prediction in the fields of molecular biology and bioinformatics are briefly overviewed herein. A method is provided to utilize intrinsic disorder knowledge to gain structural and functional information related to individual proteins, protein groups, families, classes, and even entire proteomes.

Cite

CITATION STYLE

APA

Uversky, V. N., Radivojac, P., Iakoucheva, L. M., Obradovic, Z., & Dunker, A. K. (2007). Prediction of intrinsic disorder and its use in functional proteomics. Methods in Molecular Biology (Clifton, N.J.), 408, 69–92. https://doi.org/10.1007/978-1-59745-547-3_5

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free