8. Predict the effect of each of the following environmental changes on the pKa of a glutamate side chain and explain your logic. The N-terminus of the protein is brought into the proximity of glutamic acid A lysine side chain is brought into the proximity of glutamic acid the glutamic acid side chain is shifted from the outside of the protein to the interior 9. A small protein was completely hydrolyzed and found to contain (in no particular order): Arg, Cys, Lys, Met, Phe, Thr, a. Incubation with FDNB generated Sanger Reagent yielded DNP-Lys b. Incubation with chymotrypsin had no effect on the peptide c. Incubation with trypsin yielded free arginine and lysine

8. Predict the effect of each of the following environmental changes on the pKa of a glutamate side chain and explain your logic. The N-terminus of the protein is brought into the proximity of glutamic acid A lysine side chain is brought into the proximity of glutamic acid the glutamic acid side chain is shifted from the outside of the protein to the interior 9. A small protein was completely hydrolyzed and found to contain (in no particular order): Arg, Cys, Lys, Met, Phe, Thr, a. Incubation with FDNB generated Sanger Reagent yielded DNP-Lys b. Incubation with chymotrypsin had no effect on the peptide c. Incubation with trypsin yielded free arginine and lysine

Anatomy & Physiology

1st Edition

ISBN:9781938168130

Author:Kelly A. Young, James A. Wise, Peter DeSaix, Dean H. Kruse, Brandon Poe, Eddie Johnson, Jody E. Johnson, Oksana Korol, J. Gordon Betts, Mark Womble

Publisher:Kelly A. Young, James A. Wise, Peter DeSaix, Dean H. Kruse, Brandon Poe, Eddie Johnson, Jody E. Johnson, Oksana Korol, J. Gordon Betts, Mark Womble

Chapter3: The Cellular Level Of Organization

Section: Chapter Questions

Problem 27RQ: Arrange the following terms in order of increasing specialization: oligopotency, pleuripotency,...

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1. In a protein, why does when Ala is replaced with Ile, it loses its activity but when Lys is replaced by Arg and Leu to Ile, it only has little effect on protein structure and function? Explain. 2. Why do proteins cannot be denatured reversibly when they are chemically altered to change the chemical composition of certain side chains? Explain.
don't copy 6. A protein-ligand binding reaction is run. At equilibrium, half the protein is ligand bound, the unboundligand concentration is 0.657 nM. Calculate the koff value for this reaction. Assume the kon value is typical ofprotein-ligand interactions.
Given the peptide Val-Ser-Gln-Lys The lateral chain of one of these amino acids can be modified by N-acetylation. Write the semi‐developed form of the lateral chain of this modified amino acid at pH 7 The lateral chain of one of these amino acids can be modified by phosphorylation. Write the semi‐developed form of the lateral chain of this modified amino acid at pH 7.
22-69 Indicate whether each of the following statementsrelating to protein synthesis is true or false.a. RNA is involved in both the transcription andtranslation phases of protein synthesis.b. DNA is the starting material for protein synthesis.c. The translation phase of protein synthesis convertsRNA to DNA.d. Transcription precedes translation in proteinsynthesis
Figure 16.13 An increase in phosphorylation levels of elF-2 has been observed in patients with neurodegenerative diseases such as Alzheimer’s, Parkinson's, and Huntington's. What impact do you think this might have on protein synthesis?
What property enables the residues of the amino acids serine, threonine, and tyrosine to be phosphorylated? They are polar. They are non-polar. They contain a hydroxyl group. They occur more frequently in the amino acid sequence of signaling proteins.
Arrange the following terms in order of increasing specialization: oligopotency, pleuripotency, unipotency, multipotency. multipotency, pleuripotency, oligopotency, unipotency pleuripotency, oligopotency, multipotency, unipotency oligopotency, pleuripotency, unipotency, multipotency pleuripotency, multipotency, oligopotency, unipotency
If an amino acid is not used to create new proteins, it can be ________. converted to acetyl CoA converted to glucose or ketones converted to nitrogen stored to be used later
Explain what happens if even one amino acid is substituted for another in a polypeptide chain. Provide a specific example.
A. Consider the dipeptideVal–Pro: What amino acid is the N terminal aminoacid? What amino acid is the C terminal aminoacid? How are the amino acids connected? Give the name of the dipeptide. Give the name of the dipeptide in which the amino acid order is reversed as Pro–Val.
On average, how many phosphoanhydride bonds (P;-P; bonds) are directly hydrolyzed in thecourse of synthesizing a 200 amino acid protein? Assume that you begin with the mature mRNA,ribosomal subunits, tRNAs, free amino acids, and all necessary factors.
10, 11 please answer all give the significance/role/effect of the reagent/condition in the isolation or analysis of a biomolecule. limit answers to two short sentences