Publications by authors named "Mondikalipudur Nanjappa Gounder Ponnuswamy"

Crystal structures of hemoglobin (Hb) from two flightless birds, ostrich (Struthio camelus) and turkey (Meleagris gallopova), were determined. The ostrich Hb structure was solved to a resolution of 2.22 Å, whereas two forms of turkey Hb were solved to resolutions of 1.

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Mice (Mus musculus) are nocturnal small animals belonging to the rodent family that live in burrows, an environment in which significantly high CO levels prevail. It is expected that mouse hemoglobin (Hb) plays an important role in their adaptation to living in such a high-CO environment, while many other species cannot. In the present study, mouse Hb was purified and crystallized at a physiological pH of 7 in the orthorhombic space group P222; the crystals diffracted to 2.

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Article Synopsis
  • * Mammals can be categorized based on whether they produce high or low oxygen affinity hemoglobins; however, studies on low oxygen affinity hemoglobins (like those from sheep) are less extensive.
  • * The crystal structure of sheep methemoglobin (metHb) reveals significant structural differences that contribute to its low oxygen affinity and limited response to allosteric effectors, specifically in the unique interactions at the molecular interfaces and the modified environment of its β subunits.
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In the title compound, [CoCl(C2H7N)(C3H10N2)2]Cl2, the Co(III) ion has a distorted octa-hedral coordination environment and is surrounded by four N atoms in the equatorial plane, with the other N and Cl atoms occupying the axial positions. The crystal packing is stabilized by N-H⋯Cl hydrogen bonds, forming a layered arrangement parallel to (1-10).

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In the title compound, C6H3ClN2SSe, the selenadiazole and chloro-thio-phene rings are almost coplanar [dihedral angle = 5.24 (15)°]. In the crystal, C-H⋯N inter-actions link the mol-ecules into chains extending along the b-axis direction.

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New four-coordinated tetrahedral copper(I) complexes have been synthesized from the reactions between [CuCl(2)(PPh(3))(2)] and N-(diphenylcarbamothioyl)benzamide (HL1) or N-(diethylcarbamothioyl)benzamide (HL2) in benzene. These complexes have been characterized by elemental analyses, IR, UV/Vis, (1)H, (13)C and (31)P NMR spectroscopy. The molecular structure of both the complexes, [CuCl(HL1)(2)(PPh(3))] (1) and [CuCl(HL2)(PPh(3))(2)] (2) were determined by single-crystal X-ray diffraction, which reveals distorted tetrahedral geometry around each Cu(I) ion.

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Hemoglobin is a vital protein present in almost all higher species. It is a transport protein involved in carrying oxygen from lungs to tissues and carbon dioxide back to lungs by an intrinsically coordinated manner. Even though a good amount of work has been carried out in this direction there exists scarcity of structural insight on low oxygen affinity species.

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Hemoglobin is a tetrameric, iron-containing metalloprotein, which plays a vital role in the transportation of oxygen from lungs to tissues and carbon dioxide back to lungs. Though good amount of work has already been done on hemoglobins, the scarcity of data on three dimensional structures pertaining to low oxygen affinity hemoglobins from mammalian species, motivated our group to work on this problem specifically. Herein, we report the preliminary crystallographic analysis of buffalo hemoglobin, which belongs to low oxygen affinity species.

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Hemoglobin (Hb) is a tetrameric protein, which contains four heme prosthetic groups, and each one is associated with a polypeptide chain. Herein, we report the rabbit hemoglobin which has intrinsically high oxygen affinity and possess highest sequence identity with human hemoglobin. The purified hemoglobin has been tried to crystallize in different crystallization conditions owing to its formation of various crystal systems.

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