Por favor, use este identificador para citar o enlazar a este item:
http://hdl.handle.net/10261/76066
COMPARTIR / EXPORTAR:
SHARE CORE BASE | |
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE | |
Título: | Direct measurement of barrier heights in protein folding |
Autor: | Naganathan, Athi N. CSIC ORCID; Sanchez-Ruiz, José M.; Muñoz, Víctor CSIC ORCID | Fecha de publicación: | 2005 | Editor: | American Chemical Society | Citación: | Journal of the American Chemical Society 127 (51) : 17970-17971 (2005) | Resumen: | A serious limitation in the study of protein folding reactions resides in the lack of experimental methods to measure the absolute height of the free energy barrier. This is particularly unfortunate given that if folding barriers are small, as theory predicts, it might be possible to resolve folding mechanisms directly. Here we explore the performance of a recently developed method to extract folding barriers from equilibrium differential scanning calorimetry (DSC) experiments. To test the method, we compare the thermodynamic barrier heights for 15 proteins obtained from available DSC data with the folding rates measured in kinetic experiments. The correlation between these two parameters is very good (r2 = 0.9) and has a slope consistent with the same energy scale. These results confirm that it is possible to measure free energy barriers for natural proteins from equilibrium DSC experiments. Furthermore, the measured barrier heights are small (<8 RT), in general, and marginal or nonexisting for fast-folding proteins | Descripción: | 2 páginas, 3 figuras -- PAGS nros. 17970-17971 | Versión del editor: | http://dx.doi.org/10.1021/ja055996y | URI: | http://hdl.handle.net/10261/76066 | DOI: | 10.1021/ja055996y | ISSN: | 0002-7863 | E-ISSN: | 1520-5126 |
Aparece en las colecciones: | (CIB) Artículos |
Ficheros en este ítem:
Fichero | Descripción | Tamaño | Formato | |
---|---|---|---|---|
restringido.pdf | 21,67 kB | Adobe PDF | Visualizar/Abrir |
CORE Recommender
SCOPUSTM
Citations
73
checked on 13-abr-2024
WEB OF SCIENCETM
Citations
69
checked on 18-feb-2024
Page view(s)
320
checked on 22-abr-2024
Download(s)
247
checked on 22-abr-2024
Google ScholarTM
Check
Altmetric
Altmetric
NOTA: Los ítems de Digital.CSIC están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.