Temperature-induced transitions in disordered proteins probed by NMR spectroscopy.
Methods Mol Biol
; 896: 233-47, 2012.
Article
em En
| MEDLINE
| ID: mdl-22821528
ABSTRACT
Intrinsically disordered proteins are abundant in nature and perform many important physiological functions. Multidimensional NMR spectroscopy has been crucial for the understanding of the conformational properties of disordered proteins and is increasingly used to probe their conformational ensembles. Compared to folded proteins, disordered proteins are more malleable and more easily perturbed by environmental factors. Accordingly, the experimental conditions and especially the temperature modify the structural and functional properties of disordered proteins. NMR spectroscopy allows analysis of temperature-induced structural changes at residue resolution using secondary chemical shift analysis, paramagnetic relaxation enhancement, and residual dipolar couplings. This chapter discusses practical aspects of NMR studies of temperature-induced structural changes in disordered proteins.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Temperatura
/
Proteínas
/
Ressonância Magnética Nuclear Biomolecular
Limite:
Humans
Idioma:
En
Revista:
Methods Mol Biol
Ano de publicação:
2012
Tipo de documento:
Article