BCMB30004 Lecture Notes - Lecture 15: Decoy, Tryptophan, Cyclic Adenosine Monophosphate

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orchidhare159

30 Jul 2018

School

University of Melbourne

Department

Biochemistry and Molecular Biology

Course

BCMB30004

Professor

Professor Cheng

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Document Summary

The different isoforms of pka regulatory and catalytic subunits: * there are type 1 & type 2 regulatory subunits and even these have alpha and beta which are encoded by different genes. * there are three isoforms of the catalytic subunit. * different r subunit isoforms direct pka to different subcellular locations. * so, these isoforms are localised in different regions of the cell and expressed in different tissues. * o(cid:374)(cid:272)e the holoe(cid:374)z(cid:455)(cid:373)e e(cid:374)z(cid:455)(cid:373)e (cid:271)i(cid:374)ds to (cid:272)amp the e(cid:374)z(cid:455)(cid:373)e disso(cid:272)iates a(cid:374)d that"s (cid:449)h(cid:455) the c su(cid:271)u(cid:374)it is active. The only way to inhibit the enzyme is to have something binding to the active site like a substrate such as pki or the r subunit. How does the r subunit bind camp structures of the camp-binding domains: * the r-subunit contains domains for dimerization & docking, inhibition of kinase activity and camp binding.

Related Questions

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CHECK ALL ANSWERS THAT APPLY. THERE MAY BE MORE THAN ONE ANSWERFOR EACH QUESTION. Thank you!

You know the molecular weight of the monomeric Encprotein; however you would like to get an idea of what the pI ofthe protein is. From the following options, what is the best way toestimate that?

[ ] SDS-PAGE

[ ] Size-exclusion chromatography

[ ] 2-D gel electrophoresis

[ ] "Salt out"

Protein analysis: You are attempting to separate a60-subunit protein, Enc, from a mixture of other proteins. Eachmonomer has a molecular weight of 29 kDa. At pH 7.0, the proteinhas a net charge of -12. Which of the following options is the bestway to purify this protein?

[ ] âSalt outâ via ammonium sulfate precipitation and ionexchange chromatography

[ ] Ion exchange chromatography and size-exclusionchromatography

[ ] SDS-PAGE and affinity chromatography

[ ] âSalt outâ via ammonium sulfate precipitation and affinitychromatography

I have two purified samples of the enzyme PKA (ProteinKinase A). One sample is treated with cAMP (cyclic AMP), while theother other is not. The cAMP-treated sample shows 2 bands on anon-denaturing PAGE, whereas the untreated sample shows only 1band. What is the best explanation for this result?

[ ] PKA is activated by cAMP. The active enzyme would show morebands.

[ ] PAGE causes denaturation of the PKA.

[ ] cAMP unfolds PKA.

[ ] cAMP dissociates the regulatory and catalytic subunits ofPKA.

You have some protein sample and you want to quantify itusing a spectrophotometer. You take a small sample of protein andput it in a quartz cuvette, take a wavelength scan, and observeabsorbance intensity at 280 nm. Which of the following is likely tomake it so that you can analyze protein using aspectrophotometer?

[ ] Very concentrated protein sample

[ ] Proteins are composed of chiral molecules

[ ] The number of Trp and Tyr residues found in the amino acidsequence

[ ] All of the above

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BCMB30004 Lecture Notes - Lecture 15: Decoy, Tryptophan, Cyclic Adenosine Monophosphate

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