Lecture_7-Secondary_to_Tertiary_Structure

Lecture_7-Secondary_to_Tertiary_Structure - 2 STRUCTURE SO...

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PROTEIN STRUCTURE Higher Order Structure: 2° Structure 2° STRUCTURE SO FAR α -helices • right-handed • n to n-4 H-bonding • side-chains project out and downward • 5.4Å and 3.6 residues per turn • side-chain identity and location infuence stability β -sheets • parallel and anti- parallel • more extended than α -helix • diFFerent H-bonding patterns • both types can occur in the same sheet ± β -sheets can be composed of parallel and antiparallel strands. THE β -TURN: 2 TYPES Type I Type II
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N 1 C α 1 N 2 C α 2 CO 2 N 3 C α 3 CO 3 N 4 C α 4 CO 4 CO 1 THE β -TURN: CHARACTERISTICS H-bonding occurs between the 1 st and 4 th residues the 4 th donates to the 1 st Two types of turns based on amino acid make-up Type I β -turn has any residue at position 3, except Gly Type II β -turn has a Gly at position 3 The two types differ structurally by a 180° Fip of the peptide unit linking residues 2 and 3 TERTIARY STRUCTURE Arrangements of 2° Structure GENERAL CLASSIFICATIONS OF 3° STRUCTURE
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Lecture_7-Secondary_to_Tertiary_Structure - 2 STRUCTURE SO...

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