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
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![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
0
0
Mouse 337.4
Bovine
374.7
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)/ 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?](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2Fce3589f0-5608-4fb5-a11c-ce1805f2c8e6%2Fc185a5d0-4aa6-4d73-a465-6fd964ad3294%2Fbuvklej_processed.jpeg&w=3840&q=75)
Transcribed Image Text: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
0
0
Mouse 337.4
Bovine
374.7
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)/ 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?
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