A2 Refereed review article in a scientific journal
Fluorescence-Based Protein Stability Monitoring : A Review
Authors: Gooran Negin, Kopra Kari
Publisher: MPDI
Publication year: 2024
Journal: International Journal of Molecular Sciences
Journal name in source: International Journal of Molecular Sciences
Article number: 1764
Volume: 25
Issue: 3
ISSN: 1422-0067
eISSN: 1422-0067
DOI: https://doi.org/10.3390/ijms25031764(external)
Web address : https://www.mdpi.com/1422-0067/25/3/1764(external)
Self-archived copy’s web address: https://research.utu.fi/converis/portal/detail/Publication/387005889(external)
Proteins are large biomolecules with a specific structure that is composed of one or more long amino acid chains. Correct protein structures are directly linked to their correct function, and many environmental factors can have either positive or negative effects on this structure. Thus, there is a clear need for methods enabling the study of proteins, their correct folding, and components affecting protein stability. There is a significant number of label-free methods to study protein stability. In this review, we provide a general overview of these methods, but the main focus is on fluorescence-based low-instrument and -expertise-demand techniques. Different aspects related to thermal shift assays (TSAs), also called differential scanning fluorimetry (DSF) or ThermoFluor, are introduced and compared to isothermal chemical denaturation (ICD). Finally, we discuss the challenges and comparative aspects related to these methods, as well as future opportunities and assay development directions.
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