BIOC 2580 Chapter Notes - Chapter 5: Protein Folding, Asparagine, Hydrogen Bond
14 Jun 2016
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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. Interruptions of the regular secondary structure by breaker amino acids create points of flexibility in the backbone. Folding is then largely determined by clustering of nonpolar side chains to form the core of a globular protein. The majority of proteins fold into a few distinct patterns: sandwiches. The simplest tertiary structure for a protein to adopt is a single uniform secondary structure: barrels and parallel. 4-10) is the result of folding the fibroin ( -keratin) is antiparallel -sheet (lehninger fig. 4-13) collagen forms a unique triple helical structure, the collagen helix (lehninger fig. This is not considered a generic secondary structure, since collagen helix depends on a specific repeating sequence -(gly-pro-pro)n-.
