Student Companion to Accompany Fundamentals of Biochemistry by Akif Uzman, Jerry Johnson, William Widger, Joseph Eichberg,

By Akif Uzman, Jerry Johnson, William Widger, Joseph Eichberg, Donald Voet, Judith G. Voet, Charlotte W. Pratt

Ebook annotation no longer on hand for this title...Title: .Fundamentals of Biochemistry..Author: .Uzman, Akif/ Johnson, Jerry/ Eichberg, Joseph/ Widger, William/ Voet, Donald..Publisher: .John Wiley & Sons Inc..Publication Date: .2012/01/18..Number of Pages: .257..Binding variety: .PAPERBACK..Library of Congress: .

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The standard amino acids are called α-amino acids because they have a primary amino group and a carboxyl group bound to the same carbon atom (the α carbon). Only proline has a secondary amino group attached to the α carbon, but it is still commonly referred to as an α-amino acid. 3. The generic structure of an amino acid at pH 7 is shown below. At pH 7, the amino acid is a zwitterion, or dipolar ion. A unique side chain, or R group, characterizes each amino acid. 4. Amino acids are polymerized by condensation reactions to form a chain called a polypeptide.

Both YACs and BACs can accommodate much larger pieces of foreign DNA than can plasmids. 25. The following strategy is typically used to clone a segment of DNA: (a) A fragment of DNA is obtained using restriction endonucleases that generate sticky ends. The fragment is then isolated for subsequent ligation to a vector that has been cut with the same restriction endonuclease. The vector contains two selectable genes: (i) one that allows for the selection of transformed bacteria (usually via antibiotic resistance); and (ii) another that allows for the identification of recombinant vectors (vector plus inserted DNA) among a population of transformed colonies.

The stationary phase consists of beads containing pores that span a relatively narrow size range. Smaller molecules spend more time inside the beads than larger molecules and therefore elute later (after a larger volume of mobile phase has passed through the column). Within the molecular mass range that is fractionated by the specific stationary phase used, there is a linear relationship between a substance’s elution time and the logarithm of its molecular mass. 10. Affinity chromatography exploits a protein’s specific ligand-binding behavior.

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