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Novel cyclic C<sub>5</sub>-curcuminoids possess anticancer activities against HeLa cervix carcinoma, HEC-1A adenocarcinoma, and T24 bladder carcinoma cells. [PDF]
Cancer Cell IntPandur E +5 more
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Phylogeographic Insights into <i>Aedes albopictus</i> in Korea: Integrating COX1, ND5, and CYTB Analyses. [PDF]
InsectsMonoldorova S +9 more
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Classical force field parameters for the heme prosthetic group of cytochrome c
Journal of Computational Chemistry, 2004AbstractAccurate force fields are essential for describing biological systems in a molecular dynamics simulation. To analyze the docking of the small redox protein cytochrome c (cyt c) requires simulation parameters for the heme in both the reduced and oxidized states. This work presents parameters for the partial charges and geometries for the heme in
Felix Autenrieth +3 more
semanticscholar +3 more sources
Resonance Raman scattering on the haem group of cytochrome c.
Biochemical and Biophysical Research Communications, 1973Resonance Raman spectra of the haem group of 8 × 10−5 M horse heart ferro- and ferricytochrome c solutions have been obtained. The spectra are almost identical to that of haemoglobin. The frequency of the Raman line near 1370 cm−1, which in haemoglobin is sensitive to the position of the haem iron, indicates that the iron atom of cytochrome c lies in ...
Horst Brunner
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MULTIPLE PROSTHETIC GROUPS IN CYTOCHROME C
Journal of the American Chemical Society, 1954 Martin Morrison +2 more
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Biochemistry, 2002
The yeast iso-1-cytochrome c variant Cys14Ser has been prepared in which one of the two thioether bonds by which the heme prosthetic group is normally bound to the protein has been eliminated. Comparison of the properties of this variant with those of the wild-type cytochrome provides insight into the role of this covalent attachment of the heme group ...
F. Rosell, A. Mauk
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The yeast iso-1-cytochrome c variant Cys14Ser has been prepared in which one of the two thioether bonds by which the heme prosthetic group is normally bound to the protein has been eliminated. Comparison of the properties of this variant with those of the wild-type cytochrome provides insight into the role of this covalent attachment of the heme group ...
F. Rosell, A. Mauk
semanticscholar +3 more sources
Biochimica et Biophysica Acta (BBA) - Protein Structure, 1968
Abstract 1. 1.Cytochrome c has been shown to react with salicylaldehyde at room temperature and pH 9.6 to give a cytochrome c-salicylaldehyde complex which is probably the azomethine derivative of the lysine ϵ-amino groups and the aldehyde. 2. 2.The reaction goes to completion, i.e., all 19 lysine residues react, when the ratio of aldehyde to
J N, Williams, R M, Jacobs
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Abstract 1. 1.Cytochrome c has been shown to react with salicylaldehyde at room temperature and pH 9.6 to give a cytochrome c-salicylaldehyde complex which is probably the azomethine derivative of the lysine ϵ-amino groups and the aldehyde. 2. 2.The reaction goes to completion, i.e., all 19 lysine residues react, when the ratio of aldehyde to
J N, Williams, R M, Jacobs
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Surface of Cytochromec: Infrared Spectroscopy of Carboxyl Groups
Biochemistry, 1997The carboxylate groups of organic acids give strong absorption in the infrared between approximately 1550 and 1650 cm-1. For acetate and chloroacetate derivatives, the infrared (IR) frequency of the carboxylate antisymmetric stretching mode (v(a)OCO) is related to the square root of the pK of the acid, with a shift of approximately 20 cm-1 to higher ...
W W, Wright, M, Laberge, J M, Vanderkooi
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Biochemical and Biophysical Research Communications, 1970
Abstract Cytochrome c 553 of Desulfovibrio , vulgaris differs in amino acid composition and in molecular weight (9, 100 ± 100) from cytochrome c 3 (12,000) of the same organism. This protein can be easily obtained in crystalline form. It consists of a single polypeptide chain comprising about 80 amino acid residues and bearing a single ...
Mireille Bruschi, Jean Le Gall, Karl Dus
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Abstract Cytochrome c 553 of Desulfovibrio , vulgaris differs in amino acid composition and in molecular weight (9, 100 ± 100) from cytochrome c 3 (12,000) of the same organism. This protein can be easily obtained in crystalline form. It consists of a single polypeptide chain comprising about 80 amino acid residues and bearing a single ...
Mireille Bruschi, Jean Le Gall, Karl Dus
openaire +2 more sources