2. As we've seen previously, peptide bonds involving the amino acid proline can populate both "trans" and "cis" isomers. trans-Pro cis-Pro This isomerization reaction can be the rate-limiting step in protein folding. Depending on the protein sequence, the relative favorability of the trans and cis states can change. For Pro-117 in the protein staphylococcal nuclease, the rates of the forward and reverse reactions are: ktrans-cis = 3.1 x 10-2 and keis→trans = 2.5 x 10-3 s-1. (a) What is AG" for this reaction? (b) A prolyl isomeriase enzyme increases the rate of the forward reaction to kcat,trans+cis = 2.6 s-. What is the new rate constant for the reverse reaction (kcat,cis→trans)? = 2.6 s-1, KM = 1.9 µM. If (c) This prolyl isomerase is a Michaelis-Menten enzyme with kcat you have 1 nM enzyme, what is Vo for [S]o = 0.7 µM? What about [S]o = 30 µM? For each condition, what limits the reaction speed?
2. As we've seen previously, peptide bonds involving the amino acid proline can populate both "trans" and "cis" isomers. trans-Pro cis-Pro This isomerization reaction can be the rate-limiting step in protein folding. Depending on the protein sequence, the relative favorability of the trans and cis states can change. For Pro-117 in the protein staphylococcal nuclease, the rates of the forward and reverse reactions are: ktrans-cis = 3.1 x 10-2 and keis→trans = 2.5 x 10-3 s-1. (a) What is AG" for this reaction? (b) A prolyl isomeriase enzyme increases the rate of the forward reaction to kcat,trans+cis = 2.6 s-. What is the new rate constant for the reverse reaction (kcat,cis→trans)? = 2.6 s-1, KM = 1.9 µM. If (c) This prolyl isomerase is a Michaelis-Menten enzyme with kcat you have 1 nM enzyme, what is Vo for [S]o = 0.7 µM? What about [S]o = 30 µM? For each condition, what limits the reaction speed?
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
Related questions
Question
![2. As we've seen previously, peptide bonds involving the amino acid proline can populate both "trans"
and "cis" isomers.
trans-Pro
cis-Pro
This isomerization reaction can be the rate-limiting step in protein folding. Depending on the protein
sequence, the relative favorability of the trans and cis states can change. For Pro-117 in the protein
staphylococcal nuclease, the rates of the forward and reverse reactions are: ktrans→cis = 3.1 × 10-2
and kcis→trans = 2.5 x 10-3 s-1.
(a) What is AG°' for this reaction?
(b) A prolyl isomeriase enzyme increases the rate of the forward reaction to kcat.trans->cis = 2.6 s-1.
What is the new rate constant for the reverse reaction (kcat,cis→trans)?
(c) This prolyl isomerase is a Michaelis-Menten enzyme with kcat = 2.6 s!, KM = 1.9 µuM. If
you have 1 nM enzyme, what is Vo for [S]o = 0.7 µM? What about [S]o = 30 µM? For each
condition, what limits the reaction speed?](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2Fa6c5565a-787b-43d3-b23e-780453faf6da%2F31430967-aefd-467a-9f36-db8d3d53083b%2F7xwrdeq_processed.jpeg&w=3840&q=75)
Transcribed Image Text:2. As we've seen previously, peptide bonds involving the amino acid proline can populate both "trans"
and "cis" isomers.
trans-Pro
cis-Pro
This isomerization reaction can be the rate-limiting step in protein folding. Depending on the protein
sequence, the relative favorability of the trans and cis states can change. For Pro-117 in the protein
staphylococcal nuclease, the rates of the forward and reverse reactions are: ktrans→cis = 3.1 × 10-2
and kcis→trans = 2.5 x 10-3 s-1.
(a) What is AG°' for this reaction?
(b) A prolyl isomeriase enzyme increases the rate of the forward reaction to kcat.trans->cis = 2.6 s-1.
What is the new rate constant for the reverse reaction (kcat,cis→trans)?
(c) This prolyl isomerase is a Michaelis-Menten enzyme with kcat = 2.6 s!, KM = 1.9 µuM. If
you have 1 nM enzyme, what is Vo for [S]o = 0.7 µM? What about [S]o = 30 µM? For each
condition, what limits the reaction speed?
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