Special Issue "Intrinsically Disordered Proteins in the Norm and Pathology: In-Silico Perspective"
Deadline for manuscript submissions: 31 December 2017
Prof. Dr. Lukasz Kurgan
Biomine Lab, Computer Science, Virginia Commonwealth University, Richmond, Virginia, VA 23284-3068, USA
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Phone: +1 780-492-5488
Fax: +1 780-492-1811
Interests: structural bioinformatics; intrinsically disordered proteins; structural genomics; protein function prediction; computer-aided molecular modeling; protein-ligand(drug) interactions; protein-nucleic acids interactions; protein-protein interactions; macromolecular crystallography; protein sequence analysis; microRNA; microRNA targets; conformational dynamics; big data analysis
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.
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
- 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
The below list represents only planned manuscripts. Some of these manuscripts have not been received by the Editorial Office yet. Papers submitted to MDPI journals are subject to peer-review.
Title How to study the dynamic structure of unstructured protein?-Case study of Nopp140 as an example of large intrinsically disordered protein
Authors Jung-Hyun Na1,2 and Yeon Gyu Yu1,*
Affiliations 1 Department of Chemistry, Kookmin University, Jeongneung-dong, Seongbuk-gu, Seoul 02707, Republic of Korea
2 Department of Chemistry & Nanoscience Science, Ewha Womans University, Seoul 03760, Republic of Korea
* Correspondence: email@example.com; Tel.: +82-2-910-5421
Abstract: Intrinsically disordered proteins (IDPs) represent about 30% of human genome and play key roles in the cell proliferation and cellular signaling by modulating the function of target proteins via protein-protein interactions. In addition, IDPs are related to various human diseases such as cancer, neurodegenerative diseases, and amyloidosis. To understand the molecular mechanism of IDPs, it is important to study the structural feature of IDPs during their interaction with target proteins. However, conventional biochemical and biophysical methods for analysis of protein such as X-ray crystallography have difficulty in characterizing their features since IDPs lack ordered three-dimensional structure. Here, we presented the biochemical and biophysical studies of nucleolar phosphoprotein 140 (Nopp140), which consisted of mostly disordered regions during its interaction with casein kinase 2 (CK2) that plays central roles in cell growth. The surface plasmon resonance (SPR) and electron paramagnetic resonance (EPR) studies performed to characterize the interaction between Nopp140 and CK2. Also, single-molecule fluorescence resonance energy transfer (smFRET) study revealed conformational change of Nopp140 during its interaction CK2. These studies of Nopp140 would be a good model system for understanding molecular function of IDPs.
Keywords: Intrinsically disordered protein (IDP); Nucleolar phosphoprotein 140 (Nopp140); Biophysical and biochemical studies of IDPs; Casein kinase 2 (CK2)