Human Anatomy & Physiology (11th Edition)
11th Edition
ISBN: 9780134580999
Author: Elaine N. Marieb, Katja N. Hoehn
Publisher: PEARSON
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- Write a DNA sequence that would encode the amino acid sequence valyl-tryptophanyl-lysyl-prolyl-phenylalanyl-threonine.arrow_forwardPolylysine adopts a random structure in solution at physiological pH (i.e. 7.4). Given that the e-amino group of lysine has a pKa of 10.5, under what circumstances do you think polylysine will form an a-helix? Give an explanation for your decision. Given the pKa of the side-chain COOH group, under what circumstances would you anticipate polyglutamate to form an a-helix?arrow_forwardRegarding the last answer choice, how come both alpha helices and beta sheets aren't denatured when the heat breaks peptide bonds? If heat were to break peptide bonds, wouldn't that affect the primary structure which inevitably affects the more complicated structures?arrow_forward
- The structure of an alpha helix orients the oxygens of the carbonyl group of the peptide bond towards the C-terminal end of the helix while the hydrogens of the NH groups orient toward the N-terminal end, thus imparting a dipole along the length of the helix. As a result, which kinds of amino acids would favor the C-terminal end, and which would favor the N-terminal end? negatively charged, positively charged positively charged, negatively charged negatively charged, hydrophobic positively charged, hydrophobic hydrophobic, negatively charged hydrophobic, positively chargedarrow_forwardConsider the hydrogen bonding pattern of an α-helix with the following sequence: HLRTNAGCSY Asparagine’s amide hydrogen is hydrogen bonded to: a. Serine’s side chain b. Histidine’s backbone carbonyl oxygen c. Cysteine’s backbone carbonyl oxygen d. Serine’s backbone carbonyl oxygen e. Histidine’s side chainarrow_forwardDraw the molecular formula of the covalently modifi ed histone side chain of acetyllysine. How does this modifi cation alter the chemical properties of the side chain?arrow_forward
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