Harper's Illustrated Biochemistry (Harper's Biochemistry) by Robert K. Murray, Darryl K. Granner, Peter A. Mayes, Victor

By Robert K. Murray, Darryl K. Granner, Peter A. Mayes, Victor W. Rodwell

Harper's Illustrated Biochemistry bargains concise, up to date, and authoritative assurance of the foundations of biochemistry and molecular biology as they relate to medicine.
* Revised for readability, with new streamlined association, new figures, and new on-line picture assortment * displays significant advances in biochemistry which are vital to medication * contains new chapters on amino acids and peptides, fundamental constitution of proteins, and the Human Genome undertaking * offers new and increased insurance of the mechanisms of motion of enzymes, receptors all in favour of lipoprotein metabolism and opposite ldl cholesterol shipping, RNA synthesis, gene legislation, molecular mechanisms of hormone motion, protein lifestyles cycle, and pharmacogenomics * presents medical correlations and bankruptcy summaries * gains greater than 500 transparent, descriptive illustrations

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As genes are switched on and off, proteins are synthesized in particular cell types at specific times of growth or differentiation and in response to external stimuli. Muscle cells express proteins not expressed by neural cells, and the type of subunits present in the hemoglobin tetramer undergo change pre- and postpartum. Many proteins undergo posttranslational modifications during maturation into functionally competent forms or as a means of regulating their properties. Knowledge of the human genome therefore represents only the beginning of the task of describing living organisms in molecular detail and understanding the dynamics of processes such as growth, aging, and disease.

In peptide mass profiling, for example, a peptide digest is introduced into the mass spectrometer and the sizes of the peptides are determined. A computer is then used to find an ORF whose predicted protein product would, if broken down into peptides by the cleavage method selected, produce a set of peptides whose masses match those observed by mass spectrometry. PROTEOMICS & THE PROTEOME The Goal of Proteomics Is to Identify the Entire Complement of Proteins Elaborated by a Cell Under Diverse Conditions While the sequence of the human genome is known, the picture provided by genomics alone is both static and incomplete.

The physiologically active conformation reflects the amino acid sequence, steric hindrance, and noncovalent interactions (eg, hydrogen bonding, hydrophobic interactions) between residues. Common conformations include α-helices and β-pleated sheets (see Chapter 5). ANALYSIS OF THE AMINO ACID CONTENT OF BIOLOGIC MATERIALS In order to determine the identity and quantity of each amino acid in a sample of biologic material, it is first necessary to hydrolyze the peptide bonds that link the amino acids together by treatment with hot HCl.

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