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mcb450-6f09 - Chapter 6 Proteins Secondary Tertiary and...

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Chapter 6 - Proteins: Secondary, Tertiary, and Quaternary Structure Office hours today 1:45-3:00, Noyes 208
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Ride Offered Going to Chicago via Naperville on Friday morning, 9/11. Will gladly give rides to 450 students. Email me if you want to go, giving me your cell number.
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First Hour Examination Thur, Sept 24, in class. Covers Chs. 1-12 (4 th Ed.) Do Prob. Set #1. Review old examination questions on course website.
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Forces Involved in Maintaining Higher Orders of Protein Structure Weak Interactions van der Waal’s Hydrogen bonding Ionic interactions Hydrophobic interactions
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Determination of Higher-Order Structures Information is contained in the amino acid sequence of the protein.
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Basis of Protein Structure Amide plane, shown on the next slide.
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Fig. 6-2, p. 137 Because there is no free rotation about the C-N bond, all the atoms are co-planar except for the R and H groups. Phi and psi represent variable angles of rotation.
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Fig. 6-4, p. 138 Ramachandran Plot of Allowed Rotations
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Secondary Structure Refers to regular elements, if any, present in a protein’s 3-D structure.
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Pauling’s Rules for Secondary Structure Structure is regular. The operation going between each residue in the regular structure is the same. Every peptide hydrogen and carbonyl oxygen in the peptide backbone is involved in hydrogen- bonding. Pauling envisioned two kinds of regular secondary structure: α -helix β -pleated sheet
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Alpha-Helix Regular structure with 3.6 amino acid residues per turn. A given carbonyl oxygen is H-bonded to a peptide hydrogen of the fourth amino acid down. Helix is right handed, which is thermodynamically the most stable with L- amino acids
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Sketch of α -Helix
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Fig. 6-6, p. 140 Note that sidechains protrude outward.
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Fig. 6-7, p. 141 Some Proteins With Helices (Ribbon structure depicts the polypeptide backbone.)
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Fig. 6-9, p. 141
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