Protein Unfolding Induced by Chemical Agents
A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Biochemistry".
Deadline for manuscript submissions: 31 July 2024 | Viewed by 227
Special Issue Editors
Interests: antibacterial activity; protein structures; antimicrobial proteins; glycopeptides
Special Issues, Collections and Topics in MDPI journals
Interests: protein structure and dynamics; protein-lipid interactions; cellular signaling; membrane peptides; protein folding; NMR spectroscopy
Special Issues, Collections and Topics in MDPI journals
Special Issue Information
Dear Colleagues,
Protein folding and unfolding has been an important research area since the Anfinsen dogma was established. We know that biologically important proteins work best around room temperature, atmospheric pressure, neutral pH, and in the absence of chemicals (e.g. small, organic molecules). However, the equilibrium that favours folded protein conformation can be shifted by changing any of the conditions mentioned above. Here, we aim at chemical unfolding as it has pharmaceutical importance. Importantly, folding and unfolding time scales are generally too fast for straight experimental (e.g. NMR, AFM, FRET) observations. Therefore, often the equilibria are studied by physical methods as shifted to irreversible „denatured” states. Sometimes even the unfolded states are interesting because they provide insight into the nature of disordered proteins (IDPs). In addition to experimental techniques, in-silico, molecular dynamics simulations may be of help for understanding the mechanism of chemical denaturation.
Prof. Dr. Gyula Batta
Dr. Orsolya Tőke
Guest Editors
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Keywords
- protein stability
- chemical unfolding
- denaturing conditions
- protein folding
- folding pathway
- misfolding
- conformational flexibility
- disordered state
- protein aggregation
- protein drugs
