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Special Issue "Functionally Relevant Macromolecular Interactions of Disordered Proteins 2019"
Deadline for manuscript submissions: 30 September 2019.
Prof. Dr. Istvan Simon Website E-Mail
Institute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Budapest, Hungary
Interests: protein bioinformatics; protein interactions; membrane proteins; protein stability; intrinsically disordered proteins; protein structure; protein folding; protein biophysics; protein binding; protein dynamics; protein conformation; molecular biophysics; protein refolding; membrane transport proteins; computational structural biology; structural bioinformatics
This Special Issue is the continuation of our previous special issue "Functionally Relevant Macromolecular Interactions of Disordered Proteins".
It is common that most proteins function in folded form. Another significant portion of proteins or protein segments spend a part—or sometimes most—of their time in an unstructured/disordered form. They generally fold only temporarily—typically on the surface of another protein or other macromolecule during their biochemical activity. This phenomenon has been widely studied in the past decade. However, we are expecting a great deal of new information about the functional relevance of this coupled folding and binding for this issue of IJMS. Up-to-date databases like IDEAL and DisProt are listing unstructured proteins, while ELM and DisBind are listing binding segments of this protein. A new database, Schad E et al. “DIBS: a repository of disordered binding sites mediated interactions with ordered proteins” has recently been made available in Bioinformatics: https://doi.org/10.1093/bioinformatics/btx640. A smaller but not negligible portion of disordered proteins fold via interaction with one or more disordered protein molecules. During this joint folding process, there is no template to use—the two or more polypeptide chains have to fold jointly by themselves. Since few attempts have been reported in the literature on these kinds of complexes, I kindly call your attention that the first such database Ficho E et al. “MFIB: a repository of protein complexes with mutual folding induced by binding” recently became available in Bioinformatics: https://doi.org/10.1093/bioinformatics/btx486.
Prof. Dr. Istvan Simon
Manuscript Submission Information
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- Disordered protein
- Unstructured protein
- Coupled folding and binding
- Mutual folding