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Protein folding can be described as an equilbrium between an unfolded state (U) and the folded structure (F). U=F You are studying a protein for which the AGU = -30 kJ mol-¹, (a) In the hydrophobic core of the F structure, a tyrosine side chain forms the interactions shown in the picture below. (This site is sequestered in the center of the protein no water molecules can accesss the site). You mutate the gene encoding this protein to replace the tyrosine with phenylalanine at this position. What interactions do you predict would change in the F struc- ture when you introduce this mutation? BACKSE CALRONYS BACKRUFE AMIOUS TYROSINE (b) It costs 50 kJ-mol-¹ to break a hydrogen bond in the absence of competing water molecules. Predict the value of AGF for this mutant. (e) You remeasure AGUp for the mutant protein and find it is now 0 kJ-mol-¹. Is this consistent or inconsistent with your prediction? If not, how might you explain the discrepancy?

Protein folding can be described as an equilbrium between an unfolded state (U) and the folded structure (F). U=F You are studying a protein for which the AGU = -30 kJ mol-¹, (a) In the hydrophobic core of the F structure, a tyrosine side chain forms the interactions shown in the picture below. (This site is sequestered in the center of the protein no water molecules can accesss the site). You mutate the gene encoding this protein to replace the tyrosine with phenylalanine at this position. What interactions do you predict would change in the F struc- ture when you introduce this mutation? BACKSE CALRONYS BACKRUFE AMIOUS TYROSINE (b) It costs 50 kJ-mol-¹ to break a hydrogen bond in the absence of competing water molecules. Predict the value of AGF for this mutant. (e) You remeasure AGUp for the mutant protein and find it is now 0 kJ-mol-¹. Is this consistent or inconsistent with your prediction? If not, how might you explain the discrepancy?

Biochemistry
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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3. Protein folding can be described as an equilbrium between an unfolded state (U) and the folded structure (F). U F You are studying a protein for which the AGU-30 kJ mol-¹. (a) In the hydrophobic core of the F structure, a tyrosine side chain forms the interactions shown in the picture below. (This site is sequestered in the center of the protein no water molecules can accesss the site). You mutate the gene encoding this protein to replace the tyrosine with phenylalanine at this position. What interactions do you predict would change in the F struc- ture when you introduce this mutation? BACKRUFE AMIDES INF of BACKSOSE CALRONY'S *f TYROSINE (b) It costs 50 kJ-mol-¹ to break a hydrogen bond in the absence of competing water molecules. Predict the value of AGUF for this mutant. (e) You remeasure AGU F for the mutant protein and find it is now 0 kJ mol-¹. Is this consistent or inconsistent with your prediction? If not, how might you explain the discrepancy?
Transcribed Image Text:3. Protein folding can be described as an equilbrium between an unfolded state (U) and the folded structure (F). U F You are studying a protein for which the AGU-30 kJ mol-¹. (a) In the hydrophobic core of the F structure, a tyrosine side chain forms the interactions shown in the picture below. (This site is sequestered in the center of the protein no water molecules can accesss the site). You mutate the gene encoding this protein to replace the tyrosine with phenylalanine at this position. What interactions do you predict would change in the F struc- ture when you introduce this mutation? BACKRUFE AMIDES INF of BACKSOSE CALRONY'S *f TYROSINE (b) It costs 50 kJ-mol-¹ to break a hydrogen bond in the absence of competing water molecules. Predict the value of AGUF for this mutant. (e) You remeasure AGU F for the mutant protein and find it is now 0 kJ mol-¹. Is this consistent or inconsistent with your prediction? If not, how might you explain the discrepancy?
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