In-Silico Prediction and Characterization of Intrinsic Disorder in Proteins
A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Physical Chemistry, Theoretical and Computational Chemistry".
Deadline for manuscript submissions: closed (31 May 2015) | Viewed by 96786
Special Issue Editors
Interests: bioinformatics of proteins and short RNAs; intrinsically disordered proteins; protein structure; protein-ligand interactions; protein-nucleic acids interactions; structural genomics; microRNAs; microRNA targets
Special Issues, Collections and Topics in MDPI journals
Interests: intrinsically disordered proteins; protein folding; protein misfolding; partially folded proteins; protein aggregation; protein structure; protein function; protein stability; protein biophysics; protein bioinformatics; conformational diseases; protein–ligand interactions; protein–protein interactions; liquid-liquid phase transitions
Special Issues, Collections and Topics in MDPI journals
Special Issue Information
Dear Colleagues,
The dominant dogma that proteins must fold into precise, rigid molecules to function correctly is changing. Intrinsically disordered proteins (IDPs) have at least some disordered (also called unfolded/highly flexible) regions that exist as heterogeneous ensembles of conformers. Many IDPs carry out their function without ever fully folding into a rigid molecule. They are abundant in nature, enriched in eukaryotic genomes, and crucial for numerous cellular functions, including signal transduction, regulation of cell division, transcription, translation, and many posttranslational modifications. The prevalence of disorders involving IDPs is reflected by human diseases such as cancers and cardiovascular, neurodegenerative, and genetic diseases.
Experimental annotations of IDPs are time- and resource-consuming and thus computational methods that predict and analyze disorders from protein sequences have emerged as a viable alternative to investigating IDPs. These methods find numerous important applications in functional and structural proteomics. We invite you to contribute articles that describe computational methods for predicting intrinsic disorders and their mechanisms, and the applications of computational methods to characterize the abundance, functional roles, and other characteristic features of intrinsic disorders. Articles that include an experimental component are also encouraged.
Dr. Lukasz Kurgan
Dr. Vladimir N. Uversky
Guest Editors
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Keywords
- intrinsic disorder
- intrinsically disordered proteins
- intrinsically disordered regions
- natively unfolded proteins
- natively denatured proteins
- intrinsically unstructured proteins
- intrinsically unfolded proteins
- computational prediction
- function of intrinsic disorder
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