Need the following questions answered please, thank you! People are very interested in understanding how prions fold. (Prions are proteins that beginaggregation and cause spongiform changes in the brain that result in neurodegenerativedisorders and ultimately death) The following data are for the folding (unfolded folded)) of amouse prion protein (Moulick and Udgaonkar, 2014, Biophysical Journal V 106 pp 410-420) anda Bovine prion (Hwang and Nicholson, 2018, Prion V12:5-6 pp 301-309) are provided below.Note:R= 8.314 J/molK= 0.08214atmL/molK=1.987 cal/molkSpecies Tm(K) AG(kcal/mol)at Tm00Mouse 337.4Bovine374.7AH(kcal/mol)At Tm-58-59.4AS(cal/molK) THAt Tm-172-159263.9316.2Ts271.3320.6CS Scanned with CamScannerACp(cal/molk)-790-10201. Assuming that the heat capacity is temperature independent- which protein, mouse orbovine, will be more "folded" at 310K? Which of these proteins will be more "folded" at310K? What is the fraction folded at each temperature? (Recall that AG=-RTInk and K=[U]/[F] = (1-0)/ 8 where 0 is the fraction folded)2. At what temperatures is the folding of the bovine prion enthalpically favorable?3. At which temperatures is the folding of the mouse prion entropically favorable?

People are very interested in understanding how prions fold. (Prions are proteins that begin aggregation and cause spongiform changes in the brain that result in neurodegenerative disorders and ultimately death) The following data are for the folding (unfolded folded)) of a mouse prion protein (Moulick and Udgaonkar, 2014, Biophysical Journal V 106 pp 410-420) and a Bovine prion (Hwang and Nicholson, 2018, Prion V12:5-6 pp 301-309) are provided below. Note: R= 8.314 J/molK= 0.08214atmL/molK=1.987 cal/molk Species Tm(K) AG(kcal/mol) at Tm 337.4 0 374.7 0 Mouse Bovine AH(kcal/mol) At Tm -58 -59.4 AS(cal/molk) TH At Tm -172 -159 263.9 316.2 Ts 271.3 320.6 CS Scanned with CamScanner ACp(cal/molk) -790 -1020 1. Assuming that the heat capacity is temperature independent- which protein, mouse or bovine, will be more "folded" at 310K? Which of these proteins will be more "folded" at 310K? What is the fraction folded at each temperature? (Recall that AG=-RTInK and K= [U]/[F] = (1-0)/0 where 0 is the fraction folded) 2. At what temperatures is the folding of the bovine prion enthalpically favorable? 3. At which temperatures is the folding of the mouse prion entropically favorable?

People are very interested in understanding how prions fold. (Prions are proteins that begin aggregation and cause spongiform changes in the brain that result in neurodegenerative disorders and ultimately death) The following data are for the folding (unfolded folded)) of a mouse prion protein (Moulick and Udgaonkar, 2014, Biophysical Journal V 106 pp 410-420) and a Bovine prion (Hwang and Nicholson, 2018, Prion V12:5-6 pp 301-309) are provided below. Note: R= 8.314 J/molK= 0.08214atmL/molK=1.987 cal/molk Species Tm(K) AG(kcal/mol) at Tm 337.4 0 374.7 0 Mouse Bovine AH(kcal/mol) At Tm -58 -59.4 AS(cal/molk) TH At Tm -172 -159 263.9 316.2 Ts 271.3 320.6 CS Scanned with CamScanner ACp(cal/molk) -790 -1020 1. Assuming that the heat capacity is temperature independent- which protein, mouse or bovine, will be more "folded" at 310K? Which of these proteins will be more "folded" at 310K? What is the fraction folded at each temperature? (Recall that AG=-RTInK and K= [U]/[F] = (1-0)/0 where 0 is the fraction folded) 2. At what temperatures is the folding of the bovine prion enthalpically favorable? 3. At which temperatures is the folding of the mouse prion entropically favorable?

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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Please help me with part one question 4 Thank you PDF link https://www.cusd80.com/cms/lib/AZ01001175/Centricity/Domain/8922/eofad.pdf
Three polypeptides, the sequences of which are represented below using the one-letter code for their amino acids, are present in a mixture:1. ATKNRASCLVPKHGALMFWRHKQLVSDPILQKRQHILVCRNAAG2. GPYFGDEPLDVHDEPEEG3. PHLLSAWKGMEGVGKSQSFAALIVILAOf the three, which one would migrate most slowly during chromatography through:(a) an ion-exchange resin, beads coated with positively charged groups?(b) an ion-exchange resin, beads coated with negatively charged groups?(c) a size-exclusion (gel-filtration) column designed to separate small peptides such as these?(d) Which peptide contains the ATP-binding motif shown in the following sequence logo?
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Please help me with part one questions 3,4,5 Thank you PDF link https://www.cusd80.com/cms/lib/AZ01001175/Centricity/Domain/8922/eofad.pdf
Some people have a genetic predisposition for developing priondiseases. Examples are described in Table 25.6. In the case ofGerstmann-Straüssler-Scheinker disease, the age of onset istypically 30–50 years, and the duration of the disease (whichleads to death) is about 5 years. Suggest a possible explanationwhy someone can live for a relatively long time withoutsymptoms and then succumb to the disease in a relativelyshort time.
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Cholera is caused by a toxin produced by the bacterium Vibrio cholerae. Ultimately, the toxin leads to the activation of ion channels by Protein Kinase A (PKA), indirectly causing water to leave the cell (following ions out of the cell). This loss of electrolytes and water from intestinal cells into the intestinal lumen, produces the watery diarrhea characteristic of a V.cholera infection. Would you expect lower or higher levels of PKA in cells exposed to the cholera toxin? If you were to measure CAMP levels in these cells, what would you expect to find? Why? How might the cholera toxin modify G-proteins to result in these cAMP levels?
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