Special Issue "Protein Folding 2.0"
A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Biochemistry".
Deadline for manuscript submissions: 30 November 2023 | Viewed by 1105
Special Issue Editor
2. Department of Biochemistry and Molecular Biology, Autonomous University of Barcelona, 08193 Bellaterra, Spain
Interests: protein folding; protein aggregation; protein design; high-throughput screening; bioinformatics; amyloids; Parkinson; nanomaterials; phase separation; prions; drug discovery
Special Issues, Collections and Topics in MDPI journals
Special Issue Information
Dear Colleagues,
This Special Issue is a continuation of our previous successful Special Issue “Protein Folding”.
Protein folding is among the most complex and challenging processes in biochemistry. After synthesis at the ribosome, most polypeptides must fold into their specific three-dimensional structures before they can exert any biological function. Only properly folded conformers can interact specifically with their molecular targets. Therefore, protein folding is central to many biological processes. It has long been known that the functional structure of a protein is coded by its primary one-dimensional amino acid sequence. Although the molecular mechanisms behind the folding code are not yet completely understood, we have witnessed significant advances towards this goal in recent years, resulting not only from the development of new experimental approaches and sophisticated prediction methods, but also arising from new ways of thinking about protein folding and dynamics. Folding within biomembranes, multi-domain protein folding, folding in the cell, molecular chaperone-assisted folding and the dynamics of intrinsically disordered proteins are among the newest and most active areas of research. Although protein folding and dynamics are behind virtually all cell reactions, ranging from transcription to motion, it is the link to human disease that has placed this subject in the public eye. Protein misfolding and subsequent aggregation have been shown to underlie dozens of human disorders. In order to elucidate the ways that misfolded proteins cause aggregation and cytotoxicity, it is necessary to better understand and predict protein folding. Thus, in a scientific environment that promotes technology transfer, it is encouraging to learn that the first principles approach holds the clue for therapeutic interventions in devastating disorders such as Parkinson’s and Alzheimer’s disease. The aim of this Special Issue is to illustrate frontier research in protein folding through selected works on this topic.
Prof. Dr. Salvador Ventura
Guest Editor
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 submissions that pass pre-check are 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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Keywords
- amyloid
- calorimetry
- chaperones
- crowding and folding
- downhill folding
- energy lanscape
- folding in biomembranes
- folding in the cell
- folding intermediates
- folding kinetics
- intrinsically disordered proteins
- molecular dynamics simulation of folding
- oxidative folding
- protein aggregation
- protein folding and design
- protein folding and docking
- protein folding and evolution
- protein misfolding
- single molecule folding
- transition state analysis
Related Special Issue
- Protein Folding in International Journal of Molecular Sciences (65 articles)
