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Secondary Structure – Peptides

by Kevin Ahern, PhD
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    About the Lecture

    The lecture Secondary Structure – Peptides by Kevin Ahern, PhD is from the course Biochemistry: Basics.


    Included Quiz Questions

    1. Hydrogen bonds
    2. Covalent bonds
    3. Disulfide bonds
    4. Ionic bonds
    1. Collagen
    2. Keratin
    3. Hemoglobin
    4. Myoglobin
    1. Glycine
    2. Alanine
    3. Glutamic acid
    4. Valine
    5. Isoleucine
    1. The Venkatachalam-turns consist of 20–25 amino acid residues and give a rigid shape to the proteins
    2. The β-sheet usually consists of the backbone of the β-strands extended into a zigzag arrangement resembling a series of pleats, with the peptide bonds organized in planes of alternating slopes
    3. The β-turn or reverse turn, composed of four amino acid residues, causes a change in the direction of the polypeptide chain
    4. In the α-helix, there are 3.6 amino acids per turn of the helix and each peptide bond is trans and planar
    5. In the antiparallel β-sheet, the adjacent polypeptide chains run in opposite direction; whereas, in the parallel β-sheet, the adjacent polypeptide chains run in the same direction

    Author of lecture Secondary Structure – Peptides

     Kevin Ahern, PhD

    Kevin Ahern, PhD


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