You take the PKA catalytic subunit, the regulatory subunit, and the dimerization domains and mix them in two different test tubes. One contains cAMP and one does not. You want to see if they formed a complex, so design an experiment that'd allow you if they did or did not, but you are not allowed to covalent modify any of the proteins before mixing them.

You take the PKA catalytic subunit, the regulatory subunit, and the dimerization domains and mix them in two different test tubes. One contains cAMP and one does not. You want to see if they formed a complex, so design an experiment that'd allow you if they did or did not, but you are not allowed to covalent modify any of the proteins before mixing them.

Biochemistry

9th Edition

ISBN:9781305961135

Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal

Publisher:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal

Chapter3: Amino Acids And Peptides

Section: Chapter Questions

Problem 54RE: THOUGHT QUESTION Imagine we identify a gene that is directly responsible for the effects of...

See similar textbooks

Similar questions

resting state of the protein, the Lys 216 Schiff base has pKa = 9.5 and Asp 85 has pKa = 3.5. When the conformational change occurs, the proton that was on the Schiff base moves to Asp 85. This should tell you that one or both of these two pKas changed with the conformational change. How does the pKa of Asp 85 compare with the pKa of the Lys 216 Schiff base after the conformational change?
Question: Which base (A, C, T or G) corresponds to X in the unknown? I did the experiment, got the data below, and calculated the binding constants. But I am TOTALLY lost as to how to figure this out! I don't even know what steps I would take. Base pairs Data – all had Temp = 250C PH = 7 Binding Constant A & X [A] = 0.00373221M [X] = 0.00373221M [AX] = 0.0462678M 3.322 C & X [C] = 0.0469007M [X] = 0.0469007M [CX] = 0.00309935M 1.409 T & X [T] = 0.0452279M [X] = 0.0452279M [TX] = 0.00477212M 2.333 G & X [G] = 0.0469554M [X] = 0.0469554M [GX] = 0.00304456M 2.633
Question:- What is an example of a heterotrimeric G protein and what role does it play?
THOUGHT QUESTION Imagine we identify a gene that is directly responsible for the effects of vasopressin on male mammals, including humans-we will call it trust1-that leads to the production of a vasopressin receptor in the brain, which we will call TRUST1. There are different versions of trust1, all of which lead to different levels of the behavior associated with this neuropeptide on male behavior. Give some examples where it would be a good idea to know a particular males genotype-that is, which of the trust1 genes he has. Give an example of when you think science has gone too far and this information should not be known.
Question- A strain of mutant bacterial cells lacks the enzyme uracil-DNA glycosylase. Using diagrams to show your answer, what is the consequence for the organism?
Question:- What biological rationale can explain why there are so few variants observed at position 65 of the heme distal ligand and position 94 of the heme proximal ligand of myoglobin? Why does the number of variants differ between the two sites?
Question:- The enzyme aromatase is found in the cytoplasm of some cells and converts testosterone to estrogen. You decide to test aromatase from a particular cell, and oops, your lab partner admits he drastically increased the pH in all the test tubes. Which of the following is a likely result? a. The enzyme will be denatured and the substrate will not bind to the active site. b. The enzyme will convert testosterone to estrogen at a faster rate. c. The mistake will have no effect on the experiment, because enzymes are not sensitive to pH. d. The free energy will be lowered and the reaction will not proceed spontaneously.
Effects of BPA on phosphorylation of cPLA2 in RAW264.7 cells conclusion
Question:- What is the role of tRNA? To replace T with U when transcribing mRNA. To bind the ribosome and the mRNA chain together. To transcribe the DNA and move the mRNA chain out of the nucleus. To assure that the mRNA chain carries the correct code. To carry the correct amino acids to the ribosome.
Question:- How can we determine trans-membrane domains of proteins in the absence of crystal structure?
Question for protein crystallography- 1. While performing a routine protein crystallization screening, you observe that one of your well drops has doubled in size compared to the remaining wells. Note: the drop in question was set up by taking 1 µL of the protein solution (10 mg/mL LDH in 20 mM TRIS pH 7.5, 0.5 M NaCl and 10% PEG 4000K) and adding it to 1 µL of the crystallization solution (10% PEG 4000K, 50 mM NaCl and 20 mM TRIS pH 8.0). Why did this drop grow larger in size compared to when you initially set it up?
Question:- Based on the figure below, predict what peptide bond could be the substrate of each protease(The bond marked in blue is where hydrolysis occurs, choose 2 peptides per protease type) Chymotrypsin:_________ Trypsin:_________ Elastase:_________ 1. SR−SG 2. SF−SG 3. SK−SG 4. SA−SG 5. SV−SG 6. SM−SG