BIOCHEM-ACHIEVE(FIRST DAY DISCOUNTED)
9th Edition
ISBN: 2818000069358
Author: BERG
Publisher: MAC HIGHER
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Question
Chapter 3, Problem 14P
Interpretation Introduction
Interpretation:
The strategy to develop a suitable assay for an enzyme showing a catalyzed reaction should be determined.
Concept introduction:
A peptide bond is present between the two amino acids in a protein. During the formation of a peptide bond, a molecule of water is released. The amino group of an amino acid gets associated with the carboxyl group of another. Polypeptides and proteins are the chains formed by the amino acids.
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SIGNALS 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).
Polymerase with H2N-...GMMTVPPKKKRVGMMTV...-COOH
Provide the amino acid sequence of the signal peptide
Where will this polypeptide be transported?
What is the receptor of the signal sequence?
What is the transport complex for this protein?
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…
Need help.
(a) Two ligands bind to the same site of a protein. However, when examined by ITC, for one of the ligands heat needs to be added to the system to maintain constant temperature, whereas for the other ligand, heat must be removed. Why is this the case?
Chapter 3 Solutions
BIOCHEM-ACHIEVE(FIRST DAY DISCOUNTED)
Ch. 3 - Prob. 1PCh. 3 - Prob. 2PCh. 3 - Prob. 3PCh. 3 - Prob. 4PCh. 3 - Prob. 5PCh. 3 - Prob. 6PCh. 3 - Prob. 7PCh. 3 - Prob. 8PCh. 3 - Prob. 9PCh. 3 - Prob. 10P
Ch. 3 - Prob. 11PCh. 3 - Prob. 12PCh. 3 - Prob. 13PCh. 3 - Prob. 14PCh. 3 - Prob. 15PCh. 3 - Prob. 16PCh. 3 - Prob. 17PCh. 3 - Prob. 18PCh. 3 - Prob. 19PCh. 3 - Prob. 20PCh. 3 - Prob. 21PCh. 3 - Prob. 22PCh. 3 - Prob. 23PCh. 3 - Prob. 24PCh. 3 - Prob. 25PCh. 3 - Prob. 26PCh. 3 - Prob. 27PCh. 3 - Prob. 28PCh. 3 - Prob. 29PCh. 3 - Prob. 30PCh. 3 - Prob. 31P
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- Need help. A protein X binds Ligand Y. The kon characterizing this binding is 1 x 106 M-1s-1, koff is 2 x 10-3 M-1s-1. In your in vitro X-Y binding experiment, at what concentration of Ligand Y half of the Protein X would be bound to Y. Assume that the binding is according to the Lock-and-key modelarrow_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). Catalase with H2N-...KERINGKERIANGEKSAMSKL-COOH Provide the amino acid sequence of the signal peptide Where will this polypeptide be transported? (specify the compartment) What is the name of the specific receptor of this polypeptide? The receptor may also have what alternative function?arrow_forwardIn Multi-Column Purification of rGFP. What happens to the protein amount, protein purity, and/or specific activity of a purification fraction if one of the three is changed? (i.e. understand the relationship between the three.)arrow_forward
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