Special Issue "Functionally Relevant Macromolecular Interactions of Disordered Proteins"
Deadline for manuscript submissions: closed (30 September 2018) | Viewed by 45035
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2. Center of Excellence of the Hungarian Academy of Sciences, Budapest, Hungary
Interests: protein structures; protein dynamics; protein conformation; protein folding; protein bioinformatics; protein interactions; membrane proteins; protein stability; intrinsically disordered proteins; protein biophysics; protein binding; molecular biophysics; protein refolding; membrane transport proteins; computational structural biology; structural bioinformatics
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Special Issue in International Journal of Molecular Sciences: Functionally Relevant Macromolecular Interactions of Disordered Proteins 2022
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
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- disordered protein
- unstructured protein
- coupled folding and binding
- mutual folding
- protein complex