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

By Richard A. Harvey, Denise R. Ferrier

Completely up-to-date for its 5th variation, Lippincott's Illustrated reports: Biochemistry allows scholars to speedy evaluation and assimilate quite a lot of complicated info via robust visible assets necessary to mastery of difficult biochemical thoughts. Its signature define layout, full-color illustrations, end-of-chapter summaries, and USMLE-style assessment questions make it probably the most elementary books within the box. New positive aspects contain accelerated insurance of molecular biology.A significant other web site deals 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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Each subunit has stretches of α-helical structure, and a heme-binding pocket similar to that described for myoglobin. However, the tetrameric hemoglobin molecule is structurally and functionally more complex than myoglobin. For example, hemoglobin can transport H+ and CO2 from the tissues to the lungs, and can carry four molecules of O 2 from the lungs to the cells of the body. Furthermore, the oxygen-binding properties of hemoglobin are regulated by interaction with allosteric effectors (see p.

18). 19). This altered mobility of Hb S is a result of the absence of the negatively charged glutamate residues in the two β chains, thus rendering Hb S less negative than Hb A. ] 2. ] Other symptoms include acute chest syndrome, stroke, splenic and renal dysfunction, and bone changes due to marrow hyperplasia. Heterozygotes, representing 1 in 12 African-Americans, have one normal and one sickle cell gene. The blood cells of such heterozygotes contain both Hb S and Hb A. These individuals have sickle cell trait.

It is generally accepted that the information needed for correct protein folding is contained in the primary structure of the polypeptide. Given that premise, it is difficult to explain why most proteins when denatured do not resume their native conformations under favorable environmental conditions. One answer to this problem is that a protein begins to fold in stages during its synthesis, rather than waiting for synthesis of the entire chain to be totally completed. This limits competing folding configurations made available by longer stretches of nascent peptide.

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