BIOC 2580 Lecture Notes - Lecture 7: Lactate Dehydrogenase, Triosephosphate Isomerase, Pottery Of Ancient Greece
8 Dec 2017
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Synopsis: proteins consist of polypeptide chains that fold up in a highly specific manner. The starting point for folding is the formation of secondary structure, which is a function of the amino acid sequence. The stability of proteins is dictated by internal non covalent bonds, namely hydrophobic effects, van der waals interactions (dependent of exact matching of molecular shape) and by pairing up opposite charges or hydrogen bonding partners on protein. This is not considered a generic secondary structure, since collagen helix depends on a specific repeating sequence (gly pro pro)n . Secondary structures by themselves are rigid, and give the protein an overall fibrous shape, whereas most proteins are globular. 1) clearly defined interruptions in the secondary structure; clusters of secondary structure breaker amino acids gly, pro, ser, asn asp interrupt rigid segments of secondary structure, creating more flexible turn or loop regions where the polypeptide can fold back on itself.
