dc.creator | Babul Cattán, Jorge | |
dc.creator | Stellwagen, Earle | |
dc.date.accessioned | 2018-12-20T14:36:04Z | |
dc.date.available | 2018-12-20T14:36:04Z | |
dc.date.created | 2018-12-20T14:36:04Z | |
dc.date.issued | 1972 | |
dc.identifier | Biochemistry, Volumen 11, Issue 7, 2018, Pages 1195-1200 | |
dc.identifier | 15204995 | |
dc.identifier | 00062960 | |
dc.identifier | 10.1021/bi00757a013 | |
dc.identifier | http://repositorio.uchile.cl/handle/2250/156669 | |
dc.description.abstract | Absorption spectral, circular dichroic spectral, and viscosity measurements indicate that the compact low-spin conformation characteristic of native cytochrome c is quantitatively recovered from its extended high-spin conformation at pH 2 by titration to pH 4.0. This conformational transition has a midpoint of 2.5 and is very cooperative. Comparison of the pH transitions of native and various carboxy- methylated derivatives of cytochrome c indicates that recovery of the compact conformation of the protein is coincident with coordination of histidyl-18 and does not require coordination of a second protein ligand. Extensive carboxy-methylation of cytochrome c including histidyl-18 stabilizes an unfolded high-spin conformation of the protein throughout the pH range 2-7. © 1972, American Chemical Society. All rights reserved. | |
dc.language | en | |
dc.rights | http://creativecommons.org/licenses/by-nc-nd/3.0/cl/ | |
dc.rights | Attribution-NonCommercial-NoDerivs 3.0 Chile | |
dc.source | Biochemistry | |
dc.subject | Biochemistry | |
dc.title | Participation of the Protein Ligands in the Folding of Cytochrome c | |
dc.type | Artículos de revistas | |