BIOCHEMISTRY W/1 TERM ACHEIVE ACCESS
9th Edition
ISBN: 9781319425746
Author: BERG
Publisher: MAC HIGHER
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Chapter 22, Problem 39P
Interpretation Introduction
Interpretation:
The effect on fatty acid
Concept introduction:
Protein kinase A (PKA) is a cAMP-dependent enzyme, which is various functions in the regulation of glycogen, lipid, and carbohydrate metabolism. It regulates the activity of various enzymes by phosphorylating them at specific amino acid sites. Phosphorylation is done in the presence of ATP, which acts as phosphoryl group transfer.
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Inducers and Inhibitors of AEP.
Short peptides such as legumain stabilization and activity modulation (LSAM) domain and αvβ3 integrin could enhance the activity of AEP. LSAM domain known as the prodomain of AEP blocks substrate binding before activation. This prodomain has a helical structure and two independent peptides. One is an activation peptide (AP, K287 to N323), and the other is a LSAM domain. LSAM domain remains even after AP is cleaved and released from protease at neutral pH via electrostatic interaction. AEP without LSAM domain has a lower melting temperature than AEP with LSAM domain [77, 117]. Another short peptide, αvβ3 integrin, can directly interact with AEP, and after forming a complex, the optimal pH for AEP activity is increased from 5.5 to 6.0. It indicates that αvβ3 binding could induce conformational stabilization of AEP accompanied by deprotonated C189. αvβ3 does not directly interact with the AEP active site; however, AEP docks to the αvβ3 RGD-binding site…
Chapter 22 Solutions
BIOCHEMISTRY W/1 TERM ACHEIVE ACCESS
Ch. 22 - Prob. 1PCh. 22 - Prob. 2PCh. 22 - Prob. 3PCh. 22 - Prob. 4PCh. 22 - Prob. 5PCh. 22 - Prob. 6PCh. 22 - Prob. 7PCh. 22 - Prob. 8PCh. 22 - Prob. 9PCh. 22 - Prob. 10P
Ch. 22 - Prob. 11PCh. 22 - Prob. 12PCh. 22 - Prob. 13PCh. 22 - Prob. 14PCh. 22 - Prob. 15PCh. 22 - Prob. 16PCh. 22 - Prob. 17PCh. 22 - Prob. 18PCh. 22 - Prob. 19PCh. 22 - Prob. 20PCh. 22 - Prob. 21PCh. 22 - Prob. 22PCh. 22 - Prob. 23PCh. 22 - Prob. 24PCh. 22 - Prob. 25PCh. 22 - Prob. 26PCh. 22 - Prob. 27PCh. 22 - Prob. 28PCh. 22 - Prob. 29PCh. 22 - Prob. 30PCh. 22 - Prob. 31PCh. 22 - Prob. 32PCh. 22 - Prob. 33PCh. 22 - Prob. 34PCh. 22 - Prob. 35PCh. 22 - Prob. 36PCh. 22 - Prob. 37PCh. 22 - Prob. 38PCh. 22 - Prob. 39PCh. 22 - Prob. 40PCh. 22 - Prob. 41PCh. 22 - Prob. 42PCh. 22 - Prob. 43PCh. 22 - Prob. 44PCh. 22 - Prob. 45PCh. 22 - Prob. 46PCh. 22 - Prob. 47PCh. 22 - Prob. 48PCh. 22 - Prob. 49PCh. 22 - Prob. 50PCh. 22 - Prob. 51PCh. 22 - Prob. 52PCh. 22 - Prob. 53PCh. 22 - Prob. 54PCh. 22 - Prob. 55PCh. 22 - Prob. 56PCh. 22 - Prob. 57PCh. 22 - Prob. 58PCh. 22 - Prob. 59PCh. 22 - Prob. 60PCh. 22 - Prob. 61PCh. 22 - Prob. 62P
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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 similar subjects who have not used them and that you canmeasure incidences of relapse for these subjects. Statethe null and alternative hypotheses you would use in yourstudy.arrow_forwardSIGNALS AND TARGETS. Listed below are sample polypeptides/proteins with their signal molecule/peptide. Answer the questions that follow. If you are asked to give the amino acid sequence, provide the sequence using the three-letter names of the amino acids (eg. ser-ala-met). Protease with mannose-6-phosphate Where is the receptor for this protein located? Where is the final destination of this polypeptide? What happens to the receptor after protein transport?arrow_forwardSignal transduction pathway. Sketch a G protein in the active and inactive stages, and label its parts.arrow_forward
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