BIO 1000 Lecture Notes - Lecture 9: Beta Sheet, Disulfide, Globular Protein

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Typical secondary structures are coils (an alpha helix) or folds (beta pleated sheets). The structural properties of silk are due to beta pleated sheets. The presence of so many hydrogen bonds makes each silk fiber stronger than a steel strand of the same weight. Tertiary structure is determined by interactions among various r groups. These interactions include hydrogen bonds between polar and/or charged areas, ionic bonds between charged r groups, and hydrophobic interactions and van der waals interactions among hydrophobic r groups. While these three interactions are relatively weak, strong covalent bonds called disulfide bridges that form between the sulfhydryl groups (sh) of two cysteine monomers act to rivet parts of the protein together. Quaternary structure results from the aggregation of two or more polypeptide subunits. Collagen is a fibrous protein of three polypeptides that are supercoiled like a rope. This provides structural strength for collagen"s role in connective tissue. Hemoglobin is a globular protein with quaternary structure.

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