BRS Biochemistry, Molecular Biology, & Genetics (Board - download pdf or read online

By Michael A. Lieberman, Rick Ricer

ISBN-10: 1451175361

ISBN-13: 9781451175363

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

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

Example text

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. 5. Enzymes decrease the energy of activation for a reaction. They do not affect the equilibrium concentrations of the substrates and products, nor do they change the overall Gibbs free energy change for the reaction. Clinical Thousands of diseases related to deficient or defective enzymes occur.

The types of interactions between amino acid residues that produce the three-dimensional shape of a protein include hydrophobic interactions, electrostatic interactions, and h­ ydrogen bonds, all of which are noncovalent. Covalent disulfide bonds also occur. The quaternary structure refers to the spatial arrangement of subunits in a protein that consists of more than one polypeptide chain (see Fig. 10). The subunits are joined together by the same types of noncovalent interactions that join various segments of a single chain to form its tertiary structure, as well as disulfide bonds.

Titration of amino acids a. Ionizable groups on amino acids carry protons at low pH (high [H+]), which dissociate as the pH increases. If the pH is below an ionizable group’s pKa, then the group will be protonated. Once the pH is above the pKa, the group will be deprotonated. b. 5A). 4. Dissociation of the side chains of the amino acids. 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.

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


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