P Saludjian's scientific contributions
What is this page?
This page lists the scientific contributions of an author, who either does not have a ResearchGate profile, or has not yet added these contributions to their profile.
It was automatically created by ResearchGate to create a record of this author's body of work. We create such pages to advance our goal of creating and maintaining the most comprehensive scientific repository possible. In doing so, we process publicly available (personal) data relating to the author as a member of the scientific community.
If you're a ResearchGate member, you can follow this page to keep up with this author's work.
If you are this author, and you don't want us to display this page anymore, please let us know.
It was automatically created by ResearchGate to create a record of this author's body of work. We create such pages to advance our goal of creating and maintaining the most comprehensive scientific repository possible. In doing so, we process publicly available (personal) data relating to the author as a member of the scientific community.
If you're a ResearchGate member, you can follow this page to keep up with this author's work.
If you are this author, and you don't want us to display this page anymore, please let us know.
Publications (4)
The optical rotatory dispersion of horse heart ferricytochrome c and of a ferri heme undecapeptide have been determined under various conditions. Analysis of the Soret region makes it possible to characterize three different states of ferricytochrome c. the native state (superposition of a negative and a positive Cotton effect); an intermediate sta...
Citations
... Whatever the type of lipid-protein interactions, electrostatic as in ferricytochrome c-cardiolipin, or hydrophobic as in reoxidized ferricytochrome c-cardiolipin, the circular dichroism is similar over the entire spectrum, to that of the free ferricytochrome c in the intermediate state and very different from those of ferricytochrome c in the native or denatured state. For free ferricytochrome c, the transition from the native to the intermediate state is easily achieved (increasing temperature, pH extremes, addition of external ligands) [12]. This transition does not involve a secondary structural change ; it is a result of the displacement of the sixth coordination ligand of the heme iron (side chain of methionine-80) and leads to a tertiary structural change. ...
... The spectrum of cyt c in this wavelength range contains two unambiguous markers, which describe a specific conformational states of its heme region: (i) the 695 nm band, which is characteristic for the Met80 and the heme iron bond [47,48] and (ii) the 620 nm band, of which absence or presence points to the low-spin or the high-spin states of the cyt c heme iron, respectively [49]. Changes in cyt c absorbance spectra induced by urea at pH 5 and pH 7 were significantly different from each other (Fig. 1). ...