Results 261 to 270 of about 96,012 (310)
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MAKING AND BREAKING DISULFIDE BONDS
Annual Review of Microbiology, 1997▪ Abstract It is now well established that protein folding requires the assistance of folding helpers in vivo. The formation or isomerization of disulfide bonds in proteins is a slow process requiring catalysis. In nascent polypeptide chains the cysteine residues are in the thiol form.
S, Raina, D, Missiakas
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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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Disulfide Bond Exchange in Rhodopsin
Biochemistry, 1998Rhodopsin contains two cysteines (Cys110 and Cys187) that are highly conserved among members of the G protein coupled receptor family and that form a disulfide bond connecting helixes 3 and 4 on the extracellular side of the protein. However, recent work on a rhodopsin mutant split in the cytoplasmic loop connecting helixes 3 and 4 has shown that the ...
M, Kono, H, Yu, D D, Oprian
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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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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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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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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 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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The disulfide bond formation (Dsb) system
Current Opinion in Structural Biology, 2008In oxidative folding of proteins in the bacterial periplasmic space, disulfide bonds are introduced by the oxidation system and isomerized by the reduction system. These systems utilize the oxidizing and the reducing equivalents of quinone and NADPH, respectively, that are transmitted across the cytoplasmic membrane through integral membrane components
Koreaki, Ito, Kenji, Inaba
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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
openaire +2 more sources