BIOL 1201 Lecture : Lecture 5

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15 Mar 2019
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Sequence of amino acids in protein or peptide. Determines what the protein looks like and how it functions. Core of many globulary shape and spider webs. Results from hydrogen bonding involving the peptide backbone. Alpha helix- looks like organic bonds and holds by hydrogen bonds. Beta pleated sheet- are sheets of these strands that connect to other sheets and h-bonds. Folding is due to the properties and interactions of the r groups(amino acid side chains) Hydrophobic groups minimize their interactions with water and are non-polar. The r group of the amino acid glycine is h. this makes this r group a non-polar one. Non-polar r groups are found in the interior of a protein. Sickle-cell hemoglobin mutation alters the primary, tertiary, and quaternary protein structures. Secondary has h bonds and only in the backbone(alpha or beta) Multiple polypeptide chains(subunits) fir together to form a larger protein. This will depend on what kind of protein it is.

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