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Showing 1 to 20 of 76 for “"disulfide bond"”.
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Disulfide Bond Formation: Identifying Roles of PDI Family Thiol Oxidoreductases and ER Oxidant Pathways
Protein disulfide isomerases (PDIs) catalyze the oxidation and isomerization of disulfide bonds in proteins passing through the endoplasmic reticulum (ER). Although as many as 20 enzymes are classified as PDI family members, their relative contributions to protein folding have remained an open …
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Determination of disulfide bond connecting patterns via tandem mass spectrometry (MSn) and biomolecular ion/radical reactions
<p>Disulfide bond formation is one of the most common post translational modifications to occur in proteins and naturally occurring peptides. Disulfide bond formation plays a critical role in stabilizing their three-dimensional structure; therefore, it is very important to pinpoint the correct …
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HcpE, a potential immuno-modulatory protein from Helicobacter pylori that is dependent on the Disulfide bond protein DsbHP
… in H. pylori, and demonstrated DsbHP has DiSulfide Bond (Dsb) forming activity on reduced lysozyme. Furthermore, we demonstrated that DsbHP has a DsbA-type of activity when expressed in E. coli, despite its similarity with DsbG, and that DsbHP is involved in maintaining redox homeostasis …
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The Role of Periplasmic Disulfide Bond Status in the Regulation of the Salmonella SPI1 Type Three Secretion System
… regulators: HilD, HilC and RtsA. A periplasmic disulfide bond oxidoreductase DsbA is required for SPI1 T3SS function. RtsA directly activates dsbA and deletion of dsbA leads to loss of SPI1-dependent secretion. We have studied the dsbA phenotypes by monitoring expression of SPI1 regulatory, …
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Adventitious disulfide bond formation in Escherichia coli and the involvement of thioredoxin and glutaredoxin in suppressing oxidative stress
Submission published under a 24 month embargo labeled 'Closed Access', the embargo will last until 2025-12-01
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Oxidative Protein Folding Pathways In Gram-Positive Actinobacteria
<p>Disulfide bonds are important for the stability of many secreted proteins. These covalent linkages, which result from the oxidation of neighboring cysteine (Cys) residues, are often rate-limiting steps for protein folding and maturation. Disulfide bond formation is restricted to extracellular …
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Using chemical biology as a tool to probe the mechanism of the HDL receptor
… Cys384), and the other four are connected by two disulfide bonds within the conserved Cys321-Pro322-Cys323 (CPC) motif and between Cys280 and Cys334. Converting Cys384 (but not Cys251) to serine resulted in a complete loss of BLT-1 sensitivity. In addition, single amino acid substitution at …
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The Role of Oxygen and Oxygen-Dependent Enzymes in Protein Folding, Metabolism, and Redox Homeostasis
… to utilize an oxygen dependent mechanism for disulfide bond formation required for proper folding, which represents a paradox when they are expressed under hypoxic conditions. Here we confirm the existence of oxygen independent pathways for disulfide bond formation. For the first time we …
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An investigation of the effect of cryoprotective agents on intermolecular disulfide formation
… also protect proteins against intermolecular disulfide bond formation? The model system Thiogel was used because of ease of measurement of intermolecular SS formation and lack of complicating factors found in living systems. Sulfhydryl groups on the protein molecules of Thiogel are oxidized …
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Probing static disorder in protein unfolding and chemical reactions by single-molecule force spectroscopy
… force, including protein unfolding and disulfide-bond reduction, probed at the single-molecule level. The advent of single-molecule force spectroscopy has allowed the direct measure of force-dependent reaction rates, providing a powerful approach to extract the kinetic information and to …
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3-Hydroxy-3-methylglutaryl-coenzyme A lyase: investigation of cysteines mediating intersubunit disulfide formation and regulation by thiol/disulfide exchange and discovery of an extramitochondrial homolog
… the absence of reductant, cysteine 323 forms a disulfide bond with cysteine 323 on the adjacent monomer, blocking the substrate's access to the active site which results in diminished enzyme activity. The recently published crystal structure of the human enzyme indicates that cysteines 323 on …
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Post-translational modifications of SEL24K from salmon eggs and ZPA from Xenopus laevis eggs
… for characterization of two major PTMs, disulfide bonds and glycosylation. In the first project, the disulfide bond pattern of a rhamnose-binding lectin SEL24K from the Chinook salmon Oncorhynchus tshawytscha was assigned unambiguously based on a multi-enzyme digestion strategy in …
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Patterns in the sequence context of protein disulfide bonds
Disulfide bonds play an important role in the structural stability of the proteins that contain them. Yet, little is known about the specificity with which they are formed. To address this, a representative set of disulfide bonds from nonhomologous eukaryotic polypeptides was created. The amino …
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The role of ERO1 in oxidative protein folding in the endoplasmic reticulum
The formation of native disulfide bonds is critical for the folding and stability of many secreted proteins. We describe an essential S. cerevisiae gene, ER01, which encodes a conserved ER membrane protein required for disulfide bond formation in the er .doplasmic reticulum (ER). In a conditional …
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Using High-Resolution NMR to Examine the Components that Contribute to the Activity and Stability of Phosphatase of Regenerating Liver (PRL-1) and Their Dependence on the Redox State of Cysteine Residues
… to overall physical stability. The presence of disulfide bonds most often imparts thermodynamic stability, and as such, engineered disulfide bonds have become a means for improving the viability of protein therapeutics. In some cases, however, disulfide bonds can diminish stability. PRL-1 has …
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Studies of the effect of cysteine and heme pocket mutations of the nitric oxide dioxygenase and nitrite reductase activities of human Cytoglobin and Androglobin heme domain
… free sulfhydryl and dimer with an intermolecular bond between two monomeric subunits. Biochemical studies have observed Cygb also existing as a monomer with an intramolecular disulfide bond, this form of the protein lacks crystallographic data. Adgb is a chimeric globin with a rearranged globin …
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Characterizing Factors That Influence Intracellular Thiol-Disulfide Equilibrium
<p>Thiol-disulfide balance is critical for the proper functioning of many proteins. Reduced thiol residues can aid in cofactor binding and catalysis, while disulfide bonds are often required for protein folding and stability. Therefore, oxidation of critical cysteine residues can either activate or …
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Engineering streptavidin and its target ligands with both infinite binding affinity and reversible binding capability
… the streptavidin mutein and its binding tags. Disulfide bond formation allows immobilization of tagged proteins to streptavidin. Incubation with biotin in the presence of reducing agents allows stripping off tagged proteins from streptavidin.
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ABCB6 Is a Porphyrin Transporter with a Novel Trafficking Signal That Is Conserved in Other ABC Transporters
… Moreover, we identified a novel N-terminal disulfide bond that plays an important role in the ER exit of ABCB6. This disulfide bond motif is found in other ABC family members and the loss of the conserved cysteine residue in ABCC8/SUR1 is the genetic basis for hyperinsulinemic hypoglycemia. …
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