Results 11 to 20 of about 179,181 (346)
Generally, intermolecular disulfide bond contribute to the conformational protein stability. To identify sites where intermolecular disulfide bond can be introduced into the Fab’s constant domain of the therapeutic IgG, Fab mutants were predicted using ...
Hitomi Nakamura +4 more
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Polarity of disulfide bonds [PDF]
1Department of Biochemistry and Biophysics, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599 ...
A J, Saunders, G B, Young, G J, Pielak
openaire +2 more sources
Wheat, maize, cassava, mung bean and sweet potato starches have often been added to dough systems to improve their hardness. However, inconsistent effects of these starches on the dough quality have been reported, especially in refrigerated dough.
Yu Zhou +4 more
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Background Escherichia coli (E. coli) is a promising host for production of recombinant proteins (including antibodies and antibody fragments) that don’t require complex post-translational modifications such as glycosylation.
Tomasz K. Baginski +8 more
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Disulfide bond-bridging strategy has been extensively utilized to construct tumor specificity-responsive aliphatic prodrug nanoparticles (PNPs) for precise cancer therapy.
Yuequan Wang +10 more
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Disulfide Bonds and Protein Folding [PDF]
The applications of disulfide-bond chemistry to studies of protein folding, structure, and stability are reviewed and illustrated with bovine pancreatic ribonuclease A (RNase A). After surveying the general properties and advantages of disulfide-bond studies, we illustrate the mechanism of reductive unfolding with RNase A, and discuss its application ...
W J, Wedemeyer +3 more
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Mechanisms of Disulfide Bond Formation in Nascent Polypeptides Entering the Secretory Pathway
Disulfide bonds are an abundant feature of proteins across all domains of life that are important for structure, stability, and function. In eukaryotic cells, a major site of disulfide bond formation is the endoplasmic reticulum (ER).
Philip J. Robinson, Neil J. Bulleid
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An ultralong CDRH2 in HCV neutralizing antibody demonstrates structural plasticity of antibodies against E2 glycoprotein [PDF]
A vaccine protective against diverse HCV variants is needed to control the HCV epidemic. Structures of E2 complexes with front layer-specific broadly neutralizing antibodies (bNAbs) isolated from HCV-infected individuals, revealed a disulfide bond ...
Adams +32 more
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CD44 Binding to Hyaluronic Acid Is Redox Regulated by a Labile Disulfide Bond in the Hyaluronic Acid Binding Site. [PDF]
CD44 is the primary leukocyte cell surface receptor for hyaluronic acid (HA), a component of the extracellular matrix. Enzymatic post translational cleavage of labile disulfide bonds is a mechanism by which proteins are structurally regulated by ...
Helena Kellett-Clarke +3 more
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The role of a disulfide bridge in the stability and folding kinetics of Arabidopsis thaliana cytochrome c6A [PDF]
Cytochrome c 6A is a eukaryotic member of the Class I cytochrome c family possessing a high structural homology with photosynthetic cytochrome c 6 from cyanobacteria, but structurally and functionally distinct through the presence of a disulfide bond and
Arslan +64 more
core +1 more source

