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FIGURE 11.1. The glucose carrier switches easily between two shapes.

FIGURE 11.1. The glucose carrier switches easily between two shapes. UNFIGURE 11.1. .

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FIGURE 11.1. The glucose carrier switches easily between two shapes.

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  1. FIGURE 11.1. The glucose carrier switches easily between two shapes.

  2. UNFIGURE 11.1.

  3. FIGURE 11.2. (A) The monomeric oxygen-carrying protein myoglobin. Illustration: Irving Geis. Rights owned by Howard Hughes Medical Institute. Reproduction by permission only. (B) Oxygen binding of myoglobin (in red) and hemoglobin (in purple) as oxygen pressure increases.

  4. FIGURE 11.3. A pH change that alters the charge on histidine will alter the balance of forces within a protein. At pH 6, the structure on the right will predominate.

  5. FIGURE 11.4. Phosphorylation changes the charge pattern, and hence the balance of forces within the calcium ATPase, forcing a change of shape.

  6. FIGURE 11.5. Catalysts act by reducing the activation energy (A) of a reaction.

  7. UNFIGURE 11.3.

  8. FIGURE 11.6. Definition of v0, the initial velocity of a chemical reaction.

  9. FIGURE 11.7. v0 measured in a number of reaction tubes (with [E] constant and always less than [S]) forms a hyperbolic curve when plotted as a function of substrate concentration.

  10. UNFIGURE 11.1.

  11. FIGURE 11.8. Aminotransferases use a cofactor that participates in the reaction but ends up unchanged.

  12. FIGURE 11.9. Phosphofructokinase is regulated by the binding of ATP or AMP at a regulatory site that is separate from the active site. Binding of ATP inhibits while binding of AMP activates.

  13. FIGURE 11.10. Control of Cdk1 by cyclin B and by phosphorylation.

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