Download e-book for iPad: Biochemistry, 5th Edition (Lippincott’s Illustrated Reviews) by Richard A. Harvey, Denise R. Ferrier

By Richard A. Harvey, Denise R. Ferrier

ISBN-10: 160831412X

ISBN-13: 9781608314126

Completely up to date for its 5th version, Lippincott's Illustrated experiences: Biochemistry permits scholars to quick evaluate and assimilate quite a lot of advanced info via robust visible assets necessary to mastery of difficult biochemical suggestions. Its signature define structure, full-color illustrations, end-of-chapter summaries, and USMLE-style overview questions make it essentially the most uncomplicated books within the box. New positive aspects contain extended insurance of molecular biology.A better half web site bargains totally searchable on-line textual content and extra USMLE-style questions for college students and a picture financial institution for college.

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Additional info for Biochemistry, 5th Edition (Lippincott’s Illustrated Reviews)

Example text

Thalassemias: These are defects in which the synthesis of α-globin chains is decreased or absent, typically as a result of deletional mutations. 23). If one of the four genes is defective, the individual is termed a silent carrier of α-thalassemia, because no physical manifestations of the disease occur. If two α-globin genes are defective, the individual is designated as having α-thalassemia trait. If three α-globin genes are defective, the individual has Hb H (β4) disease—a mildly to moderately severe hemolytic anemia.

Has a partial double-bond character. B. is ionized at physiologic pH. C. is cleaved by agents that denature proteins, such as organic solvents and high concentrations of urea. D. is stable to heating in strong acids. E. occurs most commonly in the cis configuration. 2 Which one of the following statements is correct? A. The α-helix can be composed of more than one polypeptide chain. B. β-Sheets exist only in the antiparallel form. C. β-Bends often contain proline. D. Domains are a type of secondary structure.

Correct answer = D. Alzheimer disease is associated with long, fibrillar protein assemblies consisting of β-pleated sheets found in the brain and elsewhere. The disease is associated with abnormal processing of a normal protein. The accumulated altered protein occurs in a β-pleated sheet configuration that is neurotoxic. The Aβ amyloid that is deposited in the brain in Alzheimer disease is derived by proteolytic cleavages from the larger amyloid precursor protein—a single transmembrane protein expressed on the cell surface in the brain and other tissues.

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Biochemistry, 5th Edition (Lippincott’s Illustrated Reviews) by Richard A. Harvey, Denise R. Ferrier


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