Prediction of Intrinsic Disorder and Its Use in Functional Proteomics
Document Type
Book Chapter
Publication Date
2007
Keywords
Intrinsically Disordered Protein, Natively Unfolded Protein, Intrinsically Unstructured Protein, Protein Flexibility, Disorder Prediction, Protein Function
Digital Object Identifier (DOI)
https://doi.org/10.1007/978-1-59745-547-3_5
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.
Was this content written or created while at USF?
Yes
Citation / Publisher Attribution
Prediction of Intrinsic Disorder and Its Use in Functional Proteomics, in M. F. Ochs (Ed.), Gene Function Analysis, Humana Press, p. 69–92
Scholar Commons Citation
Uversky, Vladimir N; Radivojac, Predrag; Iakoucheva, Lilia M.; Obradovic, Zoran; and Dunker, A. Keith, "Prediction of Intrinsic Disorder and Its Use in Functional Proteomics" (2007). Molecular Medicine Faculty Publications. 1084.
https://digitalcommons.usf.edu/mme_facpub/1084
