Pushing the limits of luminescence thermometry: probing the temperature of proteins in cells.
J Biol Phys
; 48(2): 167-175, 2022 06.
Article
em En
| MEDLINE
| ID: mdl-34997472
Proteins are involved in numerous cellular activities such as transport and catalysis. Misfolding during biosynthesis and malfunctioning as a molecular machine may lead to physiological disorders and metabolic problems. Protein folding and mechanical work may be viewed as thermodynamic energetically favorable processes in which stochastic nonequilibrium intermediate states may be present with conditions such as thermal fluctuations. In my opinion, measuring those thermal fluctuations may be a way to access the energy exchange between the protein and the physiological environment and to better understand how those nonequilibrium states may influence the misfolding/folding process and the efficiency of the molecular engine cycle. Here, I discuss luminescence thermometry as a possible way to measure those temperature fluctuations from a single-molecule experimental perspective with its current technical limitations and challenges.
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Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Luminescência
/
Termometria
Idioma:
En
Revista:
J Biol Phys
Ano de publicação:
2022
Tipo de documento:
Article
País de afiliação:
Brasil
País de publicação:
Holanda