IQUIFIB   02644
INSTITUTO DE QUIMICA Y FISICOQUIMICA BIOLOGICAS "PROF. ALEJANDRO C. PALADINI"
Unidad Ejecutora - UE
artículos
Título:
Kinetics and Thermodynamics of Membrane Protein Folding
Autor/es:
ERNESTO A. ROMAN; FRANCISCO LUIS GONZALEZ FLECHA
Revista:
Biomolecules
Editorial:
MDPI
Referencias:
Lugar: Basilea; Año: 2014 p. 354 - 373
ISSN:
2218-273X
Resumen:
Understanding protein folding has been one of the great challenges in
biochemistry and molecular biophysics. Over the past 50 years, many
thermodynamic and kinetic studies have been performed addressing the
stability of globular proteins. In comparison, advances in the membrane
protein folding field lag far behind. Although membrane proteins
constitute about a third of the proteins encoded in known genomes,
stability studies on membrane proteins have been impaired due to
experimental limitations. Furthermore, no systematic experimental
strategies are available for folding these biomolecules in vitro.
Common denaturing agents such as chaotropes usually do not work on
helical membrane proteins, and ionic detergents have been successful
denaturants only in few cases. Refolding a membrane protein seems to be a
craftsman work, which is relatively straightforward for transmembrane
β-barrel proteins but challenging for α-helical membrane proteins.
Additional complexities emerge in multidomain membrane proteins, data
interpretation being one of the most critical. In this review, we will
describe some recent efforts in understanding the folding mechanism of
membrane proteins that have been reversibly refolded allowing both
thermodynamic and kinetic analysis. This information will be discussed
in the context of current paradigms in the protein folding field.