Results 311 to 320 of about 179,181 (346)

The disulfide bond formation (Dsb) system

Current Opinion in Structural Biology, 2008
In 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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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, Federico, Katzen, Jon, Beckwith   +2 more
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Location of disulfide bonds in antithrombin III

Biological Mass Spectrometry, 1990
Proteolytic 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.
Z R, Zhou, D L, Smith
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Disulfide bond formation in proteins

1984
Publisher 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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The disulfide bonds of cobrotoxin and their relationship to lethality

Biochimica et Biophysica Acta (BBA) - Protein Structure, 1967
Abstract 1. 1. Cobrotoxin contains six disulfide bonds, and is devoid of sulfhydryl groups. 2. 2. On reduction with β-mercaptoethanol, cobrotoxin displays 11.6 to 12.0 sulfhydryl groups and loses its lethality concurrently. 3. 3. The inert, fully reduced cobrotoxin yields biologically active toxin on oxidation.
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Disulfide bonds as switches for protein function

Trends in Biochemical Sciences, 2003
The prevailing view is that disulfide bonds have been added during evolution to enhance the stability of proteins that function in a fluctuating cellular environment. However, recent evidence indicates that disulfide bonds can be more than inert structural motifs.
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Disulfide-Bond Cleavage and Formation in Proteins

Science, 1965
Disulfide bonds can be cleaved at an alkaline p H by treating a protein with excess of a reagent disulfide in the presence of catalytic amounts of thiol. The cleavage products are stable and can be isolated; they contain the mixed disulfide between the reagent and the exposed thiol groups of the protein.
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Enhancing the activity of disulfide-bond-containing proteins via promoting disulfide bond formation in Bacillus licheniformis

International Journal of Biological Macromolecules, 2023
Yangyang Zhan, Dongbo Cai
exaly  

Differentiating the effects of hydrophobic interaction and disulfide bond on the myofibrillar protein emulsion gels at the high temperature and the protein interfacial properties

Food Chemistry, 2023
Yanhong Bai, Baocai Xu
exaly  

Disulfide Bond Isomerization in Prokaryotes

Biochemistry, 2003
Annie, Hiniker, James C A, Bardwell
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