Biochemistry 2280A Lecture Notes - Lecture 4: Hydrophile, Disulfide, Cannabinoid Receptor
12 Dec 2016
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Topic 3 continued: secondary structure: take the primary sequence. The only thing we"re concerned about is the hydrogen bonding between the peptide backbones. Side chains have no involvement in this whatsoever. Two main structures form form about 50% of proteins which is why they"re covered. The side chains project outwards (they stick out of the sides of the helix) They"re stabilized by hydrogen bonds (through the amino group of the backbone of the peptide bond hydrogen bonds to nearby alpha-carbon group) Proline causes some problems here: usually not found in an alpha helix because proline wraps back around itself so that the r-side chain (bunch of hydrocarbons) binds back to amino-nitrogen. Tends to mess up alpha-helix form, so it"s rare to find one. In mice, if they lack aromatase then they"re infertile. Hydrogen bonds occur between the backbone of 2 or more separate polypeptide chains or a single polypeptide folding back on itself.
