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Cytoglobin conformations and disulfide bond formation
The FEBS Journal, 2010The oligomeric state and kinetics of ligand binding were measured for wild‐type cytoglobin. Cytoglobin has the classical globin fold, with an extension at each extremity of about 20 residues. The extended length of cytoglobin leads to an ambiguous interpretation of its oligomeric state. Although the hydrodynamic diameter corresponds to that of a dimer,
Lechauve, Christophe +7 more
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The inter-heavy chain disulfide bonds of IgG4 are in equilibrium with intra-chain disulfide bonds
Molecular Immunology, 2001Unlike other immunoglobulin G (IgG) subclasses, IgG4 antibodies in plasma have been reported to be functionally monovalent. In a previous paper, we showed that the apparent monovalency of circulating IgG4 antibodies is caused by asymmetry of plasma IgG4-a large fraction has two antigen-binding sites resulting in bispecificity.
Gerrard J Perdok +3 more
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Nondissociative Electron Capture by Disulfide Bonds
The Journal of Physical Chemistry A, 2001By means of Rydberg electron-transfer spectroscopy (RETS), negative ion photoelectron spectroscopy (NIPES), and quantum chemistry calculations, we have studied electron attachment properties of a s...
Carles, S. +8 more
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Disulfide bond formation in chloroplasts
Plant Science, 2008Abstract Regulatory protein disulfide bonds serve as key signaling elements in chloroplasts in a manner that appears independent of the generally highly reducing intra-organellar conditions. This suggests that both the formation and the reduction reactions of the disulfides are specifically catalyzed.
Gal Wittenberg, Avihai Danon
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Protein Disulfide Bond Formation in Prokaryotes
Annual Review of Biochemistry, 2003▪ Abstract Disulfide bonds formed between pairs of cysteines are important features of the structure of many proteins. Elaborate electron transfer pathways have evolved Escherichia coli to promote the formation of these covalent bonds and to ensure that the correct pairs of cysteines are joined in the final folded protein.
Hiroshi Kadokura +2 more
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Disulfide bond formation in proteins
1984Publisher Summary Protein disulfide formation in vivo as a post-translational modification is expected to depend upon both the conformation and the environment of the polypeptide chain during and after biosynthesis. Extrapolations from in vitro results may be informative, but the in vivo process should be amenable directly to study with the ...
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Post-translational control of protein function by disulfide bond cleavage.
Antioxidants and Redox Signaling, 2013Protein action in nature is largely controlled by the level of expression and by post-translational modifications. Post-translational modifications result in a proteome that is at least two orders of magnitude more diverse than the genome.
Kristina M. Cook, P. Hogg
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Biomacromolecules, 2013
Tobacco mosaic virus (TMV) is a classical viral nanoarchitecture that has been extensively employed as a promising template for the fabrication of novel nanomaterials and nanostructures.
Kun Zhou +4 more
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Tobacco mosaic virus (TMV) is a classical viral nanoarchitecture that has been extensively employed as a promising template for the fabrication of novel nanomaterials and nanostructures.
Kun Zhou +4 more
semanticscholar +1 more source
Location of disulfide bonds in antithrombin III
Biological Mass Spectrometry, 1990Proteolytic digests of human antithrombin III (ATIII) have been analyzed by a combination of reversed-phase high-performance liquid chromatography and fast atom bombardment (FAB) mass spectrometry for disulfide-containing peptides which are diagnostic for disulfide linkages in ATIII.
Zhongrui Zhou, David L. Smith
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, 2003