Chapter 4.2.3. How proteins are regulated

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Chapter 4.2.3. How proteins are regulated
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2014-10-15 16:38:25
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How proteins are regulated
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Chapter 4.2.3. How proteins are regulated.
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  1. What are the different ways that proteins are regulated.
    • 1. Allosteric regulation- (feedback inhibition product of a chain binds to regulation site slowing the rate of the reaction).
    • 2. Phosphorylation by causing conformational change stimulating (creating docking sites) or inhibiting the activity.
    • 3. Covalent modifications also control location and interaction of proteins.
  2. How does phosphorylation regulate protein function? What enzyme is used to add the phosphate group to the protein? What type of bond is used? It attracts a cluster of what and what charge do they have? How does that affect the binding of the ligand to the protein surface?


    How does phosphorylation stimulate a protein's activity into larger complexes?

    Two ways that phosphorylation inhibit or stimulate a reaction.

    How is the phosphate group introduced in the first place?
    Kinsase is used to add the phosphate group to the protein. The phosphate group covalently attaches to one or more of the protein's amino acid side chains causing a major conformational change in the protein by attracting a cluster of positively charged amino acids which in turn affects the binding of ligands elsewhere on the protein surface, altering its activity.

    The cluster of positively charged amino acids causes conformational change in the protein structure causing the ligand binding altered on the protein surface.

    By creating docking sites where other proteins can bind.

    By changing the protein's conformation and serving as docking sites for other proteins to attach.

    Through atp.
  3. A class of cell-surface, transmembrane proteins called_______.

    How do they work?

    Where do gtp-binding proteins get their phosphate groups?

    What is present when protein is active and not active?
    Receptor tyrosine kinases.

    Receptor proteins become phosphorylated serving as docking sites for binding or activation of other intracellular signaling proteins passing the signal to inside the cell.

    Gtp.

    Gtp causes activation and Gdp causes deactivation.
  4. How do proteins form large complexes that function as protein machines?

    What does the ordered assembly in single protein subunits enable?

    In this way, what happens?

    Give an example?
    By having atp driving an ordered series of conformational changes in single protein subunits.

    The ensemble of proteins to move coordinately.

    Enzymes are positioned in such a way that they carry out successive reactions in a series.

    Synthesis of proteins on a ribosome.

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