A2 Vertaisarvioitu katsausartikkeli tieteellisessä lehdessä
Fluorescence-Based Protein Stability Monitoring : A Review
Tekijät: Gooran Negin, Kopra Kari
Kustantaja: MPDI
Julkaisuvuosi: 2024
Journal: International Journal of Molecular Sciences
Tietokannassa oleva lehden nimi: International Journal of Molecular Sciences
Artikkelin numero: 1764
Vuosikerta: 25
Numero: 3
ISSN: 1422-0067
eISSN: 1422-0067
DOI: https://doi.org/10.3390/ijms25031764
Verkko-osoite: https://www.mdpi.com/1422-0067/25/3/1764
Rinnakkaistallenteen osoite: https://research.utu.fi/converis/portal/detail/Publication/387005889
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.
Ladattava julkaisu This is an electronic reprint of the original article. |  |
