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

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FIGURE (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.

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

FIGURE The glucose carrier switches easily between two shapes. UNFIGURE 11.1. FIGURE (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. FIGURE 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. FIGURE Phosphorylation changes the charge pattern, and hence the balance of forces within the calcium ATPase, forcing a change of shape. FIGURE Catalysts act by reducing the activation energy (A) of a reaction. UNFIGURE 11.3. FIGURE Definition of v 0, the initial velocity of a chemical reaction. FIGURE v 0 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. UNFIGURE 11.1. FIGURE Aminotransferases use a cofactor that participates in the reaction but ends up unchanged. FIGURE 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. FIGURE Control of Cdk1 by cyclin B and by phosphorylation.