## Abstract Potentiometric titration curves of oxidized and reduced horse heart cytochrome c in 0.15__M__ KCl at 20Β°C have been obtained by timed titration (0.125β0.500 ΞΌmol/sec) from the isoionic points (pH 10.2β10.4) to pH 3 and back to the isoionic point. Computerβassisted (PROPHET) data acquisi
Structural water in oxidized and reduced horse heart cytochrome c
β Scribed by Qi, Phoebe Xiurong ;Urbauer, Jeffrey L. ;Fuentes, Ernesto J. ;Leopold, Mary Frances ;Wand, A. Joshua
- Book ID
- 109964873
- Publisher
- Nature Publishing Group
- Year
- 1994
- Tongue
- English
- Weight
- 612 KB
- Volume
- 1
- Category
- Article
- ISSN
- 1545-9993
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
## Abstract The subβnanosecond structural dynamics of reduced and oxidized cytochrome __c__ were characterized. Dynamic properties of the protein backbone measured by amide ^15^N relaxation and side chains measured by the deuterium relaxation of methyl groups change little upon change in the redox
## Abstract The heats of ionization of protons, Ξ__H__~__i__~, of oxidized and reduced horse heart cytochrome c in 0.15__M__ KCl at 20Β°C were determined using a titration calorimeter which simultaneously afforded the potentiometric titration curve. Reproducibility of the thermal titrations is withi
## Abstract Simultaneous curve fitting for the ionization parameters of oxidized and reduced horse heart cytochrome __c__ in 0.15__M__ KCl and 20Β°C yields values for the ionization constants (as p__K__β²) and the heats of ionization (Ξ__H__~__i__~) which can reconstruct either the potentiometric or
The hydration properties of the oxidized form of horse heart cytochrome c have been studied by (1)H NMR spectroscopy. Two-dimensional, homonuclear ePHOGSY-NOESY experiments are used to map water-protein interactions. The detected NOEs reveal interactions between nonexchangeable protein protons and b