Biochemistry (Looseleaf)
9th Edition
ISBN: 9781319114800
Author: BERG
Publisher: MAC HIGHER
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Chapter 27, Problem 26P
Interpretation Introduction
Interpretation:
The effect of a mutation in PTP1B gene on type 2 diabetes patient should be determined.
Concept introduction:
Insulin is a type of anabolic hormone which is produced and secreted by islets cells of the pancreas. The main function of insulin is to control the blood glucose level in the body. It prevents the high glucose level (hyperglycemia) and low blood glucose level (hypoglycemia).
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Chapter 27 Solutions
Biochemistry (Looseleaf)
Ch. 27 - Prob. 1PCh. 27 - Prob. 2PCh. 27 - Prob. 3PCh. 27 - Prob. 4PCh. 27 - Prob. 5PCh. 27 - Prob. 6PCh. 27 - Prob. 7PCh. 27 - Prob. 8PCh. 27 - Prob. 9PCh. 27 - Prob. 10P
Ch. 27 - Prob. 11PCh. 27 - Prob. 12PCh. 27 - Prob. 13PCh. 27 - Prob. 14PCh. 27 - Prob. 15PCh. 27 - Prob. 16PCh. 27 - Prob. 17PCh. 27 - Prob. 18PCh. 27 - Prob. 19PCh. 27 - Prob. 20PCh. 27 - Prob. 21PCh. 27 - Prob. 22PCh. 27 - Prob. 23PCh. 27 - Prob. 24PCh. 27 - Prob. 25PCh. 27 - Prob. 26PCh. 27 - Prob. 27PCh. 27 - Prob. 28PCh. 27 - Prob. 29PCh. 27 - Prob. 30PCh. 27 - Prob. 31PCh. 27 - Prob. 32PCh. 27 - Prob. 33PCh. 27 - Prob. 34PCh. 27 - Prob. 35PCh. 27 - Prob. 36PCh. 27 - Prob. 37PCh. 27 - Prob. 38PCh. 27 - Prob. 39PCh. 27 - Prob. 40PCh. 27 - Prob. 41PCh. 27 - Prob. 42PCh. 27 - Prob. 43PCh. 27 - Prob. 44PCh. 27 - Prob. 45PCh. 27 - Prob. 46PCh. 27 - Prob. 47PCh. 27 - Prob. 48PCh. 27 - Prob. 49PCh. 27 - Prob. 50PCh. 27 - Prob. 51PCh. 27 - Prob. 52PCh. 27 - Prob. 53P
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- 1G. Please help me in detail. For Molecular Mechanism of ATP versus GTP selectivity of adenylate kinase, Write an expression for the reaction velocity.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_forwardLetter only. No need to discuss the answers. Please take note of the direction. Thank youarrow_forward
- 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…arrow_forwardNeed help with this. Also provided an explanation.arrow_forwardPlease help me with this question. More than one answer may be correct. THe graph relating to the information is included below. The above figures show the rate of actin polymerization in the presence of various concentration of profilin (Pfn). In the top figure, flourescence intensity is a measure of total actin that has been polymerized, and this is plotted versus time in seconds. The shade of blue of the lines in the top figure correspond to the shaded blue bars representing various concentrations of profilin in the lower figure. The lower graph shows the initial rates of polymerization of actin plotted again concentration. Which of the following is true: Question 21 options: profilin in a molecular motor profilin is a promoter of actin polymerization profilin replaced G-actin in an F-actin strand and breaks the filament profilin is an inhibitor of actin polymerization profilin binds to G-actin, preventing it from polymerizingarrow_forward
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