Combined pressure and temperature denaturation of ribonuclease A produces alternate denatured states.
Biochem Biophys Res Commun
; 473(4): 834-839, 2016 05 13.
Article
en En
| MEDLINE
| ID: mdl-27037018
ABSTRACT
Protein folding, unfolding and misfolding have become critically important to a range of health and industry applications. Increasing high temperature and high pressure are used to control and speed up reactions. A number of studies have indicated that these parameters can have a large effecton protein structure and function. Here we describe the additive effects of these parameters on the small angle scattering behaviour of ribonuclease A. We find that alternate unfolded structures can be obtained with combined high pressure and temperature treatment of the protein.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Presión
/
Desnaturalización Proteica
/
Ribonucleasa Pancreática
/
Temperatura
Idioma:
En
Revista:
Biochem Biophys Res Commun
Año:
2016
Tipo del documento:
Article