Disulfide bonding

The extrusion process frequently results in realignment of disulfide bonds and breakage of intramolecular bonds. Disulfide bonds stabilize the tertiary structure of protein and may limit protein imfolding during extrusion (Taylor et al., 2006). Flow and melt characteristics were improved when other proteins were extruded with disulfide reducing agents (Areas, 1992), which indicates that disulfide bonds adversely affect... 

Breaking Disulfide Bonds Disulfide bonds interfere with the sequencing procedure. A cystine residue (Fig. 3-7) that has one of its peptide bonds cleaved by the Edman procedure may remain attached to another polypeptide strand via its disulfide bond. Disulfide bonds also interfere with the enzymatic or chemical cleavage of the polypeptide. Two approaches to irreversible breakage of disulfide bonds are outlined in Figure 3-26. 

Elasticity Hydrophobic bonding, disulfide crosslinks Meats, baked goods Muscle proteins... 

Although all proteins are complex in structure and chiral in nature, some of them could achieve the status of a chiral selector in liquid chromatography. The complex structures of proteins are the result of the different intramolecular hydrogen-bonding, disulfide bridges, and other types of bonding. All of the proteins used for chiral resolution in liquid chromatography are obtained from animals except for cellobiohydrolase-I. The structures and properties of some of the most commonly used proteins as chiral selectors are discussed herein. 

Large molecules of molecular weights above about 50,000 may form quaternary structures by association of subunits. These structures may be stabilized by hydrogen bonds, disulfide bridges, and hydrophobic interactions. The bond energies involved in... 

Key Words Chimeric peptide cyclopeptide solid phase peptide synthesis thio-ether bond disulfide bridge herpes simplex virus glycoprotein D peptide epitope oligotuftsin carrier molecule. 

Key Words Peptide-macromolecule conjugate amide bond thioether bond disulfide bridge antibody epitope T-cell epitope peptide. 

The chemical nature of amino acids mainly dictates the contacts between them in protein stmctures in terms of hydrophobic, electrostatic, hydrogen bonding, disulfide bonds, and van der Waals inferacfions, which are key determinanfs for fhe sfructure. 

Tertiary structure involves the intramolecular folding of the polypeptide chain into a compact three-dimensional structure with a specific shape. This structure is maintained by electrovalent linkages, hydrogen bonds, disulfide bridges, van der Waals forces, and hydrophobic interactions. Hydrophobic interactions are considered to be a major force in maintaining the unique tertiary structure of proteins. 

P. aeruginosa azurin retains voltammetric interfacial electron transfer function in the adsorbed state. This is notable as the protein structure is almost certain to be modified on adsorption via the surface disulfide bond. Disulfide bond breaking followed by Au-S bond formation is thus a likely adsorption scenario, but re-assembly of the protein structure via Au-S bond formation to the liberated thiol radicals is unlikely to recover the exact native structure. 

Construction Uniform Disulfide bonded Disulfide loop... 

The tertiary structure of proteins is the three dimensional arrangement of the polypeptide chain. Tertiary structure depicts the way in which the secondary structure folds to form the three dimensional form. Different kinds of bonds or interactions are responsible for the maintenance of the tertiary structure. They include hydrophobic forces, hydrogen bonds, disulfide bonds, salt bridges, and Van der Waal forces. 

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