Lecture_6_Presentation-F11

Lecture_6_Presentation-F11 - THE -HELIX: OVERVIEW 1st type...

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PROTEIN STRUCTURE Higher Order Structure: 2° Structure THE α -HELIX: OVERVIEW 1 st type of secondary structure identiFed simplest stable 3D arrangement that a peptide sequence could achieve given the nature of the peptide bond only peptide helix that has favorable H-bonding patterns right handed R-groups found on the outside of the helix 1 turn 5.4 Å 3.6 residues The α -helix is defned by H- bonding between backbone atoms , NOT side-chain atoms!
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N CH C R 10 O H N CH C R 6 O H N CH C R 2 O H THE α -HELIX: H-BONDING PATTERN the α -helix forms readily because of optimal internal H- bonding pattern (n to n - 4) donor acceptor hydrogen bonding pattern residue ‘n’ donates a H-bond from its backbone amide to the carbonyl oxygen residues away on the amino terminal side of the peptide bond N CH C R 10 O H N CH C R 6 O H H N CH C R 2 O H - A - R - S - V - I - D - V - G - C - L - ± Residue D donates an H-bond to residue R ± Residue D accepts an H-bond from residue L - A - R - S - V - I - D - V - G - C - L - ± Residue I donates
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Lecture_6_Presentation-F11 - THE -HELIX: OVERVIEW 1st type...

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