Global ETD Search
Search theses and dissertations gathered from participating repositories worldwide. Every result links back to the library that holds it. No account is needed.
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Showing 1 to 20 of 83 for “"disulfide bonds"”.
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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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EFFECTS OF RESTRICTIVE DISULFIDE BONDS IN THE VINCULIN TAIL DOMAIN
… study, cysteine residues were inserted to form disulfide bonds to prevent motion in the arm (residues 1048-1066), strap (residues 878-896) or both regions. The ability of these mutant domains to interact with the head domain was unaffected in a fluorescence binding assay. In cosedimentation …
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The Arrangement of the Disulfide Bonds in a γG Immunoglobulin Molecule
… in the protein, indicating that there are 16 disulfide bonds. Reduction of Eu under mild conditions indicated that there were four interchain bonds, and peptides containing these bonds were isolated. A bond between half-cystines L-V and H-V links each light chain to its corresponding heavy …
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Mass Spectrometric Analysis of Thiol Proteins/Peptides Following Selenamide Derivatization And Electrolytic Reduction of Disulfide Bonds
… molecules such as electrolytic reduction of disulfide-containing peptides/proteins. In addition, electrochemistry (EC) can assist the top-down characterization of proteins by electrolytic reduction of the disulfide bonds, in which sequence coverage can be significantly improved for …
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Exploration of novel linker scaffolds enabling the simultaneous rebridging of disulfide bonds for the synthesis of antibody-drug conjugates
… which simultaneously rebridges all interchain disulfide bonds in an IgG1 antibody, has been developed and was recently reported by the Spring Group. The work reported in this thesis explores the translation of this ‘all-in-one’ rebridging linker technique to the generation of azide-containing …
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Mutable mechanics in biomaterials : a study of trichocyte keratin and Nvjp-1 protein
Disulfide bonds and metal-coordination bonds serve as flexible connections on account of their variable bond strengths in different chemical environments. Both bonds can act as an effective switch to stabilize or weaken a protein's geometry. These mechanisms are responsible for protein mutability, …
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Thiol-Disulfide Exchange in Human Growth Hormone
… protein aggregation. The formation of non-native disulfide bonds is a common route to covalent aggregation of therapeutic proteins and other biologics [2, 3]. Disulfide bonds participate in hydrolytic and oxidative degradation reactions that form non-native disulfide bonds and other reactive …
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Disulfide Cross -Linking in Protein Microspheres
… of the microsphere shell. Treatment with a disulfide reductant established that disulfide bonds are the covalent cross-link between protein molecules. Mass spectrometry has shown that inter-protein disulfide bonding is not random. The disulfide bonds that do form reflect the electrostatic …
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Evolution as a design tool to inform biomolecular engineering
… thermal stability of an enzyme by engineering disulfide bonds and electrostatic salt bridges on the surface of the enzyme. Two methods to assist disulfide engineering were developed- 1) A neural network model to predict disulfide bonds within existing structures from mutual information and a …
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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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Post-translational processing of the low density lipoprotein receptor
… reticulum, the LDL receptor folds and forms disulfide bonds in multiple cysteine-rich repeats. N- and 0-linked oligosaccharide chains are added in the endoplasmic reticulum and processed during passage through the Golgi apparatus, en route to the cell surface. The aim of this thesis was to …
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Extrusion performance and physicochemical characterization of texturized native and chemically modified whey proteins in carbohydrate-containing systems
… controlled. An optimum between the presence of disulfide bonds and hydrophobic interactions to form a properly texturized product from whey protein isolates was observed. Disulfide bonds contributed to the formation of hard, non cohesive products, whereas hydrophobic interactions resulted in …
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Top Down Mass Spectrometry of Archaea and Human Tumor Cells
… and internal acetylations, methylations, disulfide bonds, and protein truncations. Proteins were also characterized with known coding single nucleotide polymorphisms, alternative splice variants, and highly homologous gene family members.
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Stimuli-Responsive Polymer Systems that Respond to Redox Potential and pH for Controlled Drug Release
… a glutathione (GSH) sensitive bond, typically disulfide bonds, for intracellular activation or degradation. In these documented series of experiments, I first focus on poly(disulfide)s and report on the synthesis of fully degradable poly(disulfide) cross-linked nanogel drug carriers formed by …
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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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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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Sonochemically-produced proteinaceous microspheres
… by sonochemically generated superoxide to form disulfide bonds.
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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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Improving Structural Features Prediction in Protein Structure Modeling
… features, such as secondary structures, disulfide bonds, and solvent accessibility is a critical intermediate step stone to obtain correct three-dimensional models ultimately.</p> <p>In this dissertation, we report a set of approaches for improving the accuracy of structural features …
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Development of high throughput screening systems for the efficient production of antibody fragments in Escherichia coli
… in soluble and active form in the absence of disulfide bonds. This was achieved using a strain incapable of forming disulfide bonds in proteins expressed in its periplasm in combination with the APEx 2-hybrid system. The selected clones exhibited higher solubility, activity, and stability than …
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