Special Issue "Intrinsically Disordered Proteins in the Norm and Pathology: In-Silico Perspective"
Deadline for manuscript submissions: closed (31 December 2017)
Assoc. Prof. Dr. Vladimir N. Uversky
Molecular Medicine, University of South Florida, Tampa, USA
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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
Intrinsically disordered proteins (IDPs) and hybrid proteins that have ordered domains and intrinsically disordered regions (IDRs) are proteins and regions that do not have stable tertiary and/or secondary structures under physiological conditions. They are very common in nature and functionally complement ordered proteins. Despite being devoid of unique structures, IDPs/IDPRs are important players in regulation, signaling, and control, they engage in binding to multiple partners, and participate in one-to-many and many-to-one signaling. Being crucial controllers of numerous biological processes, IDPs/IDPRs are tightly controlled and precisely tuned themselves by multiple means, including alternative splicing and posttranslational modifications. There are numerous examples showing that when de-regulated and uncontrolled, various IDPs/IDPRs are involved in the development of various pathological conditions, such as amyloidoses, cancers, cardiovascular disease, diabetes, genetic diseases, neurodegenerative diseases, psychiatric diseases, and many other maladies. IDPs/IDPRs are nowadays being considered as new and very promising drug targets.
Computational methods for prediction and analysis of disorder from protein sequences, for performing analysis of protein dynamics, as well as for finding correlation between intrinsic disorder and various human diseases, have emerged as viable approaches greatly enhancing research capabilities of modern protein scientists. These methods find numerous important applications in functional and structural proteomics. We invite you to contribute articles that describe computational methods for predicting IDPs/IDPRs, their functions and pathological associations, and the applications of computational methods to characterize the abundance, functional roles, conformational dynamics, and other characteristic features of intrinsically disordered proteins. 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.
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- intrinsic disorder
- intrinsically disordered proteins
- intrinsically disordered regions
- computational prediction
- function of intrinsic disorder
- protein-protein interactions
- posttranslational modifications
- alternative splicing
- induced folding
- protein misfolding
- protein aggregation
- gain of pathological function
- point mutation
- drug discovery