BIOCHEMISTRY (LOOSELEAF)-W/ACCESS
9th Edition
ISBN: 9781319425784
Author: BERG
Publisher: Macmillan Higher Education
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Chapter 25, Problem 25P
Interpretation Introduction
Interpretation:
The standard free energy of the binding of methotrexate using the given three proteins and the decrease in BE due to each mutation needs to be determined.
Concept introduction:
Proteins are chains of amino acid joined with polypeptide bonds. Each protein has an active site in its native functional structure. In this active site, few amino acids interact with the ligands. Mutation in these amino acids can lead to functional change of the protein.
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Crohn’s disease. Omega-3 fatty acids have been tested asa means to prevent relapse of Crohn’s disease. Two large,randomized, placebo-controlled studies have shown nosuch benefit from omega-3 fatty acids. Suppose you areasked to design an experiment to further study this claim.Imagine that you have collected data on Crohn’s relapsesin subjects who have used these omega-3 fatty acids and
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Draw the structure.
Saccharide X occurs in the roots of several species of plants. Deduce the structure of saccharide x from the following data:
1. Acidic hydrolysis of 1 mol of stachyose yields 2 mol of D-galactose, 1 mol of D-glucose, and 1 mol of D-fructose.
2. Stachyose is a nonreducing sugar.
3. Treating stachyose with an a-galactosidase produces a mixture containing D-galactose, sucrose, and a nonreducing trisaccharide called
raffinose.
4. Acidic hydrolysis of raffinose gives D-glucose, D-fructose, and D-galactose. Treating raffinose with an a-galactosidase yields D-galactose
and sucrose. Treating raffinose with invertase (an enzyme that hydrolyzes sucrose) yields fructose and melibiose
5. Methylation of saccharide x followed by hydrolysis yields 2,3,4,6-tetra-O-methyl-D-galactose, 2,3,4-tri-0-methyl-D-galactose,
2,3,4-tri-O-methyl-D-glucose, and 1,3,4,6-tetra-O-methyl-D-fructose.
Chemical labeling of chymotrypsin by the compound tosylphenylalanine chloromethyl ketone (TPCK) modifies the His 57 in the
enzyme's active site. The structure of this derivative is shown below. TPCK inactivates the enzyme because the bulky addition
prevents it from cleaving nearby covalent bonds.
HCI
+ CH,
C-O
Chymotrypsin-His 57 TPCK
Modified enzyme
True
O False
Chapter 25 Solutions
BIOCHEMISTRY (LOOSELEAF)-W/ACCESS
Ch. 25 - Prob. 1PCh. 25 - Prob. 2PCh. 25 - Prob. 3PCh. 25 - Prob. 4PCh. 25 - Prob. 5PCh. 25 - Prob. 6PCh. 25 - Prob. 7PCh. 25 - Prob. 8PCh. 25 - Prob. 9PCh. 25 - Prob. 10P
Ch. 25 - Prob. 11PCh. 25 - Prob. 12PCh. 25 - Prob. 13PCh. 25 - Prob. 14PCh. 25 - Prob. 15PCh. 25 - Prob. 16PCh. 25 - Prob. 17PCh. 25 - Prob. 18PCh. 25 - Prob. 19PCh. 25 - Prob. 20PCh. 25 - Prob. 21PCh. 25 - Prob. 22PCh. 25 - Prob. 23PCh. 25 - Prob. 24PCh. 25 - Prob. 25PCh. 25 - Prob. 26PCh. 25 - Prob. 27PCh. 25 - Prob. 28PCh. 25 - Prob. 29PCh. 25 - Prob. 30PCh. 25 - Prob. 31PCh. 25 - Prob. 32PCh. 25 - Prob. 33PCh. 25 - Prob. 34PCh. 25 - Prob. 35PCh. 25 - Prob. 36PCh. 25 - Prob. 37PCh. 25 - Prob. 38PCh. 25 - Prob. 39PCh. 25 - Prob. 40PCh. 25 - Prob. 41PCh. 25 - Prob. 42PCh. 25 - Prob. 43PCh. 25 - Prob. 44PCh. 25 - Prob. 45PCh. 25 - Prob. 46PCh. 25 - Prob. 47PCh. 25 - Prob. 48PCh. 25 - Prob. 49PCh. 25 - Prob. 50PCh. 25 - Prob. 51P
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