Document Type
Article
Publication Date
2013
Keywords
Cis-trans Isomerization, Conformational Restriction, Intrinsically Disordered Protein, Post-translational Modification, Protein Solubility, Protein Surfaces
Digital Object Identifier (DOI)
https://doi.org/10.4161/idp.24360
Abstract
A significant fraction of every proteome is occupied by biologically active proteins that do not form unique three-dimensional structures. These intrinsically disordered proteins (IDPs) and IDP regions (IDPRs) have essential biological functions and are characterized by extensive structural plasticity. Such structural and functional behavior is encoded in the amino acid sequences of IDPs/IDPRs, which are enriched in disorder-promoting residues and depleted in order-promoting residues. In fact, amino acid residues can be arranged according to their disorder-promoting tendency to form an alphabet of intrinsic disorder that defines the structural complexity and diversity of IDPs/IDPRs. This review is the first in a series of publications dedicated to the roles that different amino acid residues play in defining the phenomenon of protein intrinsic disorder. We start with proline because data suggests that of the 20 common amino acid residues, this one is the most disorder-promoting.
Rights Information
This work is licensed under a Creative Commons Attribution-Noncommercial 3.0 License
Was this content written or created while at USF?
Yes
Citation / Publisher Attribution
Intrinsically Disordered Proteins, v. 1, issue 1, art. e24360
Scholar Commons Citation
Theillet, Francois-Xavier; Kalmar, Lajos; Tompa, Peter; Han, Kyou-Hoon; Selenko, Philipp; Dunker, A. Keith; Daughdrill, Gary W.; and Uversky, Vladimir N., "The Alphabet of Intrinsic Disorder: I. Act Like a Pro: On the Abundance and Roles of Proline Residues in Intrinsically Disordered Proteins" (2013). Molecular Medicine Faculty Publications. 583.
https://digitalcommons.usf.edu/mme_facpub/583
