341lecture04sept16sakai

341lecture04sept16sakai - Cell Biology 341 Last lecture:...

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Cell Biology 341 Weds., Sept. 16, 2009 Today: Four levels of protein structure: primary, secondary, tertiary and quaternary Noncovalent interactions determine higher levels of protein structure The α helix and β sheet of secondary structure Last lecture: Van der Waals attractions Hydrophobic forces 4 types of macromolecules Amino acids are linked by peptide bonds in proteins Behavior of amphipathic lipids (fatty acids, phospholipids) in aqueous solution = hydrophobic interactions Chapter 3: Examples of protein function
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Primary Structure Each protein contains a unique sequence of amino acids which is exactly the same in all molecules of the protein This linear sequence of amino acids linked by covalent peptide bonds is called the primary structure The differing properties of the 20 different amino acid side chains, and the sequence in which they occur, ultimately determine the overall structure of the protein This overall structure is largely determined by noncovalent bonds and interactions
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Examples of three types of noncovalent bonds in proteins: H-bonds can occur between atoms of two peptide bonds (secondary structure) , between atoms of a peptide bond and a side chain,
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This note was uploaded on 12/05/2009 for the course BIO 341 taught by Professor Noris during the Fall '09 term at Rhode Island.

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341lecture04sept16sakai - Cell Biology 341 Last lecture:...

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