C.. The formation of a hydrogen bonding dimer of N-methylacetamide has been studied as a model for hydrogen bonding in proteins. The thermodynamic parameters (at 298 K) measured for this process in water are shown below. 2 H3C CH3 N-methylacetamide H3C Fo ---- HN H3C HN CH3 CH3 AG° 3.1 kcal mol-1 AH° 0.0 kcal mol-1 AS-10 cal mol-1 K-1 N-methylacetamide hydrogen-bonded dimer a) Provide a molecular level reasoning for the value of AH and sign of AS° for this process. b) The conclusion below may be drawn from these data. Explain how his conclusion is reached. Hydrogen bonds are unlikely to be a strong stabilizing factor for a protein folding in water. c) Do you agree with this conclusion? What might be a limitation of this model for describing protein folding? d) It is well known that hydrogen bonds are prevalent in folded protein structures, so they appear to be important. So, if this conclusion is correct, what is an alternative possible role of hydrogen bonds in protein folding?
C.. The formation of a hydrogen bonding dimer of N-methylacetamide has been studied as a model for hydrogen bonding in proteins. The thermodynamic parameters (at 298 K) measured for this process in water are shown below. 2 H3C CH3 N-methylacetamide H3C Fo ---- HN H3C HN CH3 CH3 AG° 3.1 kcal mol-1 AH° 0.0 kcal mol-1 AS-10 cal mol-1 K-1 N-methylacetamide hydrogen-bonded dimer a) Provide a molecular level reasoning for the value of AH and sign of AS° for this process. b) The conclusion below may be drawn from these data. Explain how his conclusion is reached. Hydrogen bonds are unlikely to be a strong stabilizing factor for a protein folding in water. c) Do you agree with this conclusion? What might be a limitation of this model for describing protein folding? d) It is well known that hydrogen bonds are prevalent in folded protein structures, so they appear to be important. So, if this conclusion is correct, what is an alternative possible role of hydrogen bonds in protein folding?
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
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Step 1: Favorability of thermodynamic parameters
VIEWStep 2: (a) Molecular reasoning for observed standard change in enthalpy and entropy for H-bonding in NMA
VIEWStep 3: (b) Explanation for the given conclusion
VIEWStep 4: (c) The limitations of NMA model for protein folding and why it is wrong
VIEWStep 5: (d) An alternate role for H-bonds in protein backbone as it folds
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