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.