Studying protein stability in crowded environments by NMR.
Prog Nucl Magn Reson Spectrosc
; 140-141: 42-48, 2024.
Article
em En
| MEDLINE
| ID: mdl-38705635
ABSTRACT
Most proteins perform their functions in crowded and complex cellular environments where weak interactions are ubiquitous between biomolecules. These complex environments can modulate the protein folding energy landscape and hence affect protein stability. NMR is a nondestructive and effective method to quantify the kinetics and equilibrium thermodynamic stability of proteins at an atomic level within crowded environments and living cells. Here, we review NMR methods that can be used to measure protein stability, as well as findings of studies on protein stability in crowded environments mimicked by polymer and protein crowders and in living cells. The important effects of chemical interactions on protein stability are highlighted and compared to spatial excluded volume effects.
Palavras-chave
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas
/
Ressonância Magnética Nuclear Biomolecular
/
Estabilidade Proteica
Limite:
Humans
Idioma:
En
Revista:
Prog Nucl Magn Reson Spectrosc
Ano de publicação:
2024
Tipo de documento:
Article