BIOL 2021 Lecture Notes - Lecture 3: Pectin, Cytoskeleton, Glycerol
12 May 2013
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Document Summary
Always asymmetric: this is because of the asymmetry created when pattern is synthesized by er. Alpha helix: helix that crosses the membrane. In order for stabilization, there are a lot of hydrophobic amino acids within the membrane: single pass or multi pass transmembrane protein (1 vs. 3 on figure) Beta-barrel: beta sheet polypeptide that has been rolled up into a barrel, ancient protein type, special locations. Chloroplasts: form pores, important as transport proteins and act as receptors, h-bonds between strands (b-pleated sheets, 8-20 strands passing through the system. In both alpha-helicies and beta-barrels, the polar h-bonding groups in the peptide bond make internal h bonds with other peptide bonds. In a disordered chain, the peptide polar groups are not bounded to each other or lipids: a disordered peptide chain, thus, increases the free energy and is thus less favoured. Disulphide bonds on exterior chain: cystiene s s bonds, always on the outside.
