Biochemistry of Collagen

by Kevin Ahern, PhD

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    Now, the strands of collagen are made originally in the endoplasmic reticulum of cells. That’s where the synthesis of collagen begins. Within the endoplasmic reticulum, the hydroxylation of proline and lysine side chains that occurs and this is critical both for the release of the collagen from the cell and also in providing the strength that’s necessary for the collagen to support all the different things that we described. The hydroxylation that occurs on these two amino acids is necessary as I said for secretion. If something happens at hydroxylation and prevents it from happening then the collagen chain will not be released from the cell. The secreted collagen chains form a helix spontaneously on their own as they are being released. The helices, as I said, cross-link for strength, meaning that they form chemical bonds between each other. Now, this slide shows the amino acid sequence of a portion of one of the chains. This is what we call the primary structures we’ve described earlier and other things about protein. It contains the sequence of amino acids. As we look at this sequence, we can see some interesting things. There are three amino acids that jump out, the first of those being hydroxyproline. Hydroxyproline is shown as the Hpr in this diagram. Hydroxyproline is not a natural amino acid. It’s formed by the chemical modification of proline which occurs after the collagen has been made. It’s called a post-translational modification. Hydroxyproline doesn’t occur in too many proteins. Proline, we also noticed is very abundant within this region of the collagen primary chain. This abundance of proline is particularly unusual for a helical type protein because proline in most proteins forms bends and bends are not consistent with a helical structure. The third amino acid that’s very abundant here is...

    About the Lecture

    The lecture Biochemistry of Collagen by Kevin Ahern, PhD is from the course RNA and the Genetic Code. It contains the following chapters:

    • Biochemistry of Collagen
    • Hydroxylation of Proline
    • Prolyl Hydroxylase

    Included Quiz Questions

    1. It occurs in the endoplasmic reticulum.
    2. It prevents the release from the cell.
    3. It occurs on arginines and alanines.
    4. All of the answers are true.
    5. None of the answers are true.
    1. ...glycine.
    2. ...proline.
    3. ...hydroxyproline.
    4. ...lysine.
    5. ...hydroxylysine.
    1. It gives collagen more thermal stability.
    2. It occurs after export from the cell.
    3. It directly requires vitamin C.
    4. All of the answers are true.
    5. None of the answers are true.
    1. It uses molecular oxygen in its catalysis.
    2. It converts proline to hydroxylysine.
    3. It reduces iron to Fe++ in its catalysis.
    4. All of the answers are true.
    5. None of the answers are true.
    1. All of the answers are true.
    2. None of the answers are true.
    3. It is found in the endoplasmic reticulum.
    4. It catalyzes a reaction necessary for collagen export.
    5. It catalyzes the most abundant post-translational modification in the body.

    Author of lecture Biochemistry of Collagen

     Kevin Ahern, PhD

    Kevin Ahern, PhD

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