Special Issue "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)
Dr. Lukasz Kurgan
Electrical and Computer Engineering, University of Alberta, Edmonton, Canada
Website | E-Mail
Fax: +1 780-492-1811
Interests: bioinformatics of proteins and short RNAs; intrinsically disordered proteins; protein structure; protein-ligand interactions; protein-nucleic acids interactions; structural genomics; microRNAs; microRNA targets
Assoc. Prof. Dr. Vladimir N. Uversky
Molecular Medicine, University of South Florida, Tampa, USA
Website | E-Mail
Interests: intrinsically disordered proteins; protein folding; protein misfolding; partially folded proteins; protein aggregation; protein structure; protein function; protein biophysics; protein bioinformatics; conformational diseases; protein–ligand interactions; protein–protein interactions
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
Manuscript Submission Information
Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All papers will be peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.
Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. International Journal of Molecular Sciences is an international peer-reviewed open access monthly journal published by MDPI.
Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 1800 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.
- 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