BIOC 2300 Lecture Notes - Lecture 6: Alpha Helix, Protein Folding, Beta Sheet
25 Jan 2019
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Bioc2300 lecture 6: secondary, tertiary and quaternary protein structure. 4 different levels of protein structure: primary structure: 3d packing of entire protein: quaternary structure: Proteins are able to fold on their own. Because they are complex molecules, we break them down in terms of structure. Every protein has a nh and a carboxyl, and these are quite polar. Tfor them to exist within the hydrophobic inside of a protein, they need to be stable. Backbone the simplest but not that informative (a trace of just the alpha carbons). The wireframe (stick model), all atoms are shown. Spacefill shows the surface the van der waal radii of all the atoms, and ribbon diagrams highlights certain aspects of secondary structure. Alpha helices are spiral and beta sheets are flat arrows. Peptide bonds limit conformational flexibility: each amino acid residue along the polypeptide backbone contributes three bonds:
