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Disulfide Bond Formation in Peptides
Current Protocols in Protein Science, 2001AbstractThe formation of disulfide bridges is often a crucial final stage in peptide synthesis. There is compelling evidence that the disulfide pattern can be critical in the folding and structural stabilization of many natural peptide and protein sequences, while the artificial introduction of disulfide bridges into natural or designed peptides may ...
Lin, Chen, Ioana, Annis, George, Barany
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Thiol–Disulfide Exchange in Signaling: Disulfide Bonds As a Switch
Antioxidants & Redox Signaling, 2013The major function of disulfide bonds is not only the stabilization of protein structures. Over the last 30 years, a change in perspective took place driven by groundbreaking experiments, which promoted disulfide bonds to central players in essential thiol-disulfide exchange reactions involved in signal transduction, thiol protection, and redox ...
Messens, Joris, Collet, Jean François
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2,2′-Dithiobispyrazine: about the disulfide bond
Acta Crystallographica Section C Structural Chemistry, 2023X-ray diffraction studies reveal that pyrazine-2-thiol undergoes condensation to 2,2′-dithiobispyrazine [systematic name: 2-(pyrazin-2-yldisulfanyl)pyrazine], C8H6N4S2 (I), under aerial conditions. In the molecule of I, the pyrazine rings are arranged in an almost perpendicular manner, with an absolute value of the C—S—S—C torsion angle of −91.45 (6)°.
Kinga Wzgarda-Raj +3 more
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The Characteristics of Disulfide‐Centered Hydrogen Bonds
Angewandte Chemie, 2021AbstractThe disulfide‐centered hydrogen bonds in the three different model systems of diethyl disulfide⋅⋅⋅H2O/H2CO/HCONH2 clusters were characterized by high‐resolution Fourier transform microwave spectroscopy and quantum chemical computations. The global minimum energy structures for each cluster are experimentally observed and are characterized by ...
Xiaolong Li +6 more
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Disulfide Bonding in Protein Biophysics
Annual Review of Biophysics, 2012It has been known for many decades that cell surface, soluble-secreted, and extracellular matrix proteins are generally rich in disulfide bonds, but only more recently has the functional diversity of disulfide bonding in extracellular proteins been appreciated.
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Disulfide Bond in Diethyl Disulfide: A Rotational Spectroscopic Study
The Journal of Physical Chemistry A, 2018Diethyl disulfide was investigated by pulsed jet Fourier transform microwave spectroscopy. The spectroscopic study was complemented by ab initio calculations. The first two most stable conformers predicted at the MP2/6-311++G(d,p) level of theory were observed in the supersonic expansion. Two 13C and one 34S isotopologues for the most stable conformer (
Jiaqi Zhang +3 more
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How Proteins Form Disulfide Bonds
Antioxidants & Redox Signaling, 2011The identification of protein disulfide isomerase, almost 50 years ago, opened the way to the study of oxidative protein folding. Oxidative protein folding refers to the composite process by which a protein recovers both its native structure and its native disulfide bonds.
Depuydt, Matthieu +2 more
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2013
Numerous methods have been developed for the formation of disulfide bonds in recombinant DNA-derived and chemically synthesized peptides and proteins, but only a few have found widespread acceptance. The choice of method(s) for formation of disulfide in synthetic peptides and proteins needs to be tailored for each individual polypeptide in such a way ...
Fazel, Shabanpoor +3 more
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Numerous methods have been developed for the formation of disulfide bonds in recombinant DNA-derived and chemically synthesized peptides and proteins, but only a few have found widespread acceptance. The choice of method(s) for formation of disulfide in synthetic peptides and proteins needs to be tailored for each individual polypeptide in such a way ...
Fazel, Shabanpoor +3 more
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The disulfide bond in carboxypeptidase A: A
Biochemical and Biophysical Research Communications, 1969Abstract Carboxypeptidase A was assayed for active sulfhydryl groups by titration with HgCl 2 . A chloride ion probe NMR technique was utilized to observe the behavior of the mercuric ion. Although mercuric ion was found to bind to the enzyme, it could be removed by dialysis showing that the binding cannot be through a sulfur atom.
Robert G. Bryant +2 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.
J, Schuurman +3 more
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