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Proton resonance assignments of horse ferricytochrome c.
Feng Y, Roder H, Englander SW, Wand AJ, Di Stefano DL. Feng Y, et al. Among authors: roder h. Biochemistry. 1989 Jan 10;28(1):195-203. doi: 10.1021/bi00427a027. Biochemistry. 1989. PMID: 2539855
As starting points for the assignment of the oxidized protein, a limited set of protons was initially assigned by use of 2D NMR magnetization transfer methods to correlate resonances in the oxidized form with assigned resonances in the reduced form [Wand, A. J., Di Stefano, D. L. …
As starting points for the assignment of the oxidized protein, a limited set of protons was initially assigned by use of 2D NMR magnetizatio …
Kinetic mechanism of cytochrome c folding: involvement of the heme and its ligands.
Elöve GA, Bhuyan AK, Roder H. Elöve GA, et al. Among authors: roder h. Biochemistry. 1994 Jun 7;33(22):6925-35. doi: 10.1021/bi00188a023. Biochemistry. 1994. PMID: 8204626
The observation of a single highly protected (140-fold) backbone amide, that of His 18, suggests the presence of a persistent H-bond consistent with heme ligation of the His 18 side chain in the unfolded state. ...A fast kinetic phase (80 s-1) accompanied by a major decrea …
The observation of a single highly protected (140-fold) backbone amide, that of His 18, suggests the presence of a persistent H-bond …
289 results