Michael A. Lieberman, Rick Ricer's BRS Biochemistry, Molecular Biology, & Genetics (Board PDF

By Michael A. Lieberman, Rick Ricer

ISBN-10: 1451175361

ISBN-13: 9781451175363

BRS Biochemistry, Molecular Biology, and Genetics is a superb reduction for USMLE Step 1 education and for coursework in biochemistry, molecular biology, and genetics. absolutely up to date for its 6th variation, chapters are written in an overview structure and contain pedagogical positive factors reminiscent of bolded key phrases, figures, tables, algorithms, and highlighted scientific correlates. USMLE-style questions and solutions persist with each one bankruptcy and a finished examination seems to be on the finish of the ebook.

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Additional info for BRS Biochemistry, Molecular Biology, & Genetics (Board Review Series) (6th Edition)

Example text

As the pH increases, the charge on the side chain goes from zero to negative or from positive to zero. The pKa is the pH at which one-half of the molecules of an amino acid in solution have side chains that are charged. The other half are uncharged. B. 0 COOH Equivalents of OH – added A. 5. Titration curves for glycine (A) and histidine (B). The molecular species of glycine present at various pHs are indicated by the molecules above the curve. For histidine, pKa2 is the dissociation constant of the imidazole (side chain) group.

General properties of enzymes The reactions of the cell would not occur rapidly enough to sustain life if enzyme catalysts were 1. not present. Substrates bind at the active sites of enzymes, where they are converted to products and released. 3. Enzymes are usually highly specific for their substrates and products. a. Many enzymes recognize only a single compound as a substrate. b. Some enzymes, such as those involved in digestion, are less specific. 4. Many enzymes require cofactors that frequently are metal ions or derivatives of vitamins.

The free enzyme and the substrate) or reacts (to release the product and regenerate the free enzyme): k1 k3 E + S  ES → E + P k2 where E is the enzyme, S is the substrate, ES is the enzyme–substrate complex, P is the product, and k1, k2, and k3 are rate constants. 2. From this concept, the Michaelis–Menten equation was derived: v= Vmax[S] Km + [S] where Km = (k2 + k3)/k1 and Vmax is the maximum velocity. 3. The rate of formation of products (the velocity of the reaction) is related to the concentration of the enzyme–substrate complex: v = k3[ES] Vmax is reached when all of the enzyme is in the enzyme–substrate complex.

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BRS Biochemistry, Molecular Biology, & Genetics (Board Review Series) (6th Edition) by Michael A. Lieberman, Rick Ricer


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