Download e-book for kindle: Elsevier's Integrated Review Biochemistry: With STUDENT by John W. Pelley PhD

By John W. Pelley PhD

ISBN-10: 0323074464

ISBN-13: 9780323074469

Effectively merge easy technological know-how and scientific abilities with Elsevier's built-in overview Biochemistry, by way of John W. Pelley, PhD. This concise, high-yield identify within the renowned built-in assessment sequence makes a speciality of the center wisdom in biochemistry whereas linking that info to similar recommendations from different simple technological know-how disciplines. Case-based questions on the finish of every bankruptcy provide help to gauge your mastery of the fabric, and a color-coded layout helps you to fast locate the explicit information you would like. on-line entry through - incorporated together with your buy - permits you to comfortably entry the book's entire textual content and illustrations on-line in addition to suitable content material from different scholar seek advice titles. This concise and undemanding reference offers the most important information for the early years of clinical education and USMLE preparation.

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Additional resources for Elsevier's Integrated Review Biochemistry: With STUDENT CONSULT Online Access, 2e

Example text

3-2). , dipeptide [two amino acids] or oligopeptide [relatively few amino acids]). The properties of a polypeptide are determined by the side chains of their amino acids. PATHOLOGY Hemoglobin Mutations Sickle cell hemoglobin (HbS) and hemoglobin C (HbC) both have single amino acid substitutions in residue 6 of the bglobin. Sickle cell globin has a nonpolar substitution (valine) for the normal polar residue (glutamate), whereas hemoglobin C has a polar substitution (lysine) for the polar glutamate.

L A single substrate (S) binds reversibly to form the enzyme substrate complex, ES. KEY POINTS ABOUT ACTIVE SITE PROPERTIES n Amino acid residues of the active site may be far apart in the primary structure owing to the folding required for tertiary structure. n The active site is induced to undergo a change in conformation when the substrates bind. n The requirements for substrate binding are so specific that the amino acids forming the active site for the same enzyme are highly conserved between different species.

L Affinity labels are substrate analogs that react with one or more of the amino acids that make up the active site; sequence determination of the labeled enzyme allows identification of active site amino acids. l X-ray diffraction analysis with either the substrate or a transition state analog bound to an active site reveals spatial relationships within the active site. l Site-directed mutagenesis creates mutant enzymes with amino acid substitutions at active sites; substitutions that alter normal activity help identify amino acids crucial to the active site.

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Elsevier's Integrated Review Biochemistry: With STUDENT CONSULT Online Access, 2e by John W. Pelley PhD

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