2. The diagram to the right shows the change in the structure of the C-terminal portion of each of the ẞ-subu- nits of human hemoglobin (HbA) in the oxyHb to deox- yHb or R-to-T transition. The hydrogen bonding interac- tion of the C-terminal ẞHis 146 residue with the side chain of Asp94, highlighted by the red ellipse, has been shown to be responsible for a major portion of the proton uptake associated with the Bohr effect. Treatment of HbA with the enzyme carboxypeptidase A (CPA) results in loss of the C-terminal ẞHis 146 and ẞTyr145 residues of the ẞ- subunits. (a) ( ) Draw a Hill plot [log(Y/[1-Y]) vs. log(pO2), Y = fraction of heme groups occupied by O2] to compare the values of the Hill coefficient nн and the O2-binding affinity at pH 7.4 of normal HbA before and after treat- ment of with CPA. (b) (' ) How will the plot for CPA-digested HbA change at pH 7.2? (c) 1 Hi5146 HN- ✓ Low PK B-chain. CH2 CH-NH-CO-CH-NH- CH₂ Tyr145 он HbO2 or R state Туг145 CH-CH2- OH co NH CH CH₂ His Cy593 HS-CH=CH-NH-CO- Co NH -CH-CH Cy593 ASP94 HS-CR CH-NH-CO- CO N-H...O NH HN -CH2-CH High pk Asp94 B-chain. deoxyHb or T state Anesthetic gases used in surgery are known to bind to the hemoglobin molecule in red blood cells. The diagram below illustrates O2 binding curves of normal human HbA in the presence of the anesthetic gas dichloromethane (DCM). % OXYGENATION 100 • UNTREATED DCM 10 Torr 80 DCM 23 Torr DCM 50 Torr × DCM 100 Torr 60 40 Effect of dichloromethane (DCM) on 02 binding curves of HbA. Symbols: O, 0 Torr DCM; +, 10 Torr DCM; , 23 Torr DCM; A, 50 Torr DCM; x, 100 Torr DCM. (1 Torr = 1 mm Hg.) The solutions were buffered to pH 7.4. 20 1 0.5 1.0 log pО2 1.5 2.0
2. The diagram to the right shows the change in the structure of the C-terminal portion of each of the ẞ-subu- nits of human hemoglobin (HbA) in the oxyHb to deox- yHb or R-to-T transition. The hydrogen bonding interac- tion of the C-terminal ẞHis 146 residue with the side chain of Asp94, highlighted by the red ellipse, has been shown to be responsible for a major portion of the proton uptake associated with the Bohr effect. Treatment of HbA with the enzyme carboxypeptidase A (CPA) results in loss of the C-terminal ẞHis 146 and ẞTyr145 residues of the ẞ- subunits. (a) ( ) Draw a Hill plot [log(Y/[1-Y]) vs. log(pO2), Y = fraction of heme groups occupied by O2] to compare the values of the Hill coefficient nн and the O2-binding affinity at pH 7.4 of normal HbA before and after treat- ment of with CPA. (b) (' ) How will the plot for CPA-digested HbA change at pH 7.2? (c) 1 Hi5146 HN- ✓ Low PK B-chain. CH2 CH-NH-CO-CH-NH- CH₂ Tyr145 он HbO2 or R state Туг145 CH-CH2- OH co NH CH CH₂ His Cy593 HS-CH=CH-NH-CO- Co NH -CH-CH Cy593 ASP94 HS-CR CH-NH-CO- CO N-H...O NH HN -CH2-CH High pk Asp94 B-chain. deoxyHb or T state Anesthetic gases used in surgery are known to bind to the hemoglobin molecule in red blood cells. The diagram below illustrates O2 binding curves of normal human HbA in the presence of the anesthetic gas dichloromethane (DCM). % OXYGENATION 100 • UNTREATED DCM 10 Torr 80 DCM 23 Torr DCM 50 Torr × DCM 100 Torr 60 40 Effect of dichloromethane (DCM) on 02 binding curves of HbA. Symbols: O, 0 Torr DCM; +, 10 Torr DCM; , 23 Torr DCM; A, 50 Torr DCM; x, 100 Torr DCM. (1 Torr = 1 mm Hg.) The solutions were buffered to pH 7.4. 20 1 0.5 1.0 log pО2 1.5 2.0
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. The diagram to the right shows the change in the
structure of the C-terminal portion of each of the ẞ-subu-
nits of human hemoglobin (HbA) in the oxyHb to deox-
yHb or R-to-T transition. The hydrogen bonding interac-
tion of the C-terminal ẞHis 146 residue with the side chain
of Asp94, highlighted by the red ellipse, has been shown
to be responsible for a major portion of the proton uptake
associated with the Bohr effect. Treatment of HbA with
the enzyme carboxypeptidase A (CPA) results in loss of
the C-terminal ẞHis 146 and ẞTyr145 residues of the ẞ-
subunits.
(a) ( ) Draw a Hill plot [log(Y/[1-Y]) vs. log(pO2), Y
= fraction of heme groups occupied by O2] to compare
the values of the Hill coefficient nн and the O2-binding
affinity at pH 7.4 of normal HbA before and after treat-
ment of with CPA.
(b) ('
) How will the plot for CPA-digested HbA
change at pH 7.2?
(c) 1
Hi5146
HN-
✓ Low PK
B-chain.
CH2
CH-NH-CO-CH-NH-
CH₂
Tyr145
он
HbO2
or R state
Туг145
CH-CH2-
OH
co
NH
CH
CH₂
His
Cy593
HS-CH=CH-NH-CO-
Co
NH
-CH-CH
Cy593
ASP94
HS-CR CH-NH-CO-
CO
N-H...O
NH
HN
-CH2-CH
High pk
Asp94
B-chain.
deoxyHb
or T state
Anesthetic gases used in surgery are known to bind to the hemoglobin molecule in red
blood cells. The diagram below illustrates O2 binding curves of normal human HbA in the presence of
the anesthetic gas dichloromethane (DCM).
% OXYGENATION
100
• UNTREATED
DCM 10 Torr
80
DCM 23 Torr
DCM 50 Torr
× DCM 100 Torr
60
40
Effect of dichloromethane (DCM) on
02 binding curves of HbA.
Symbols: O, 0 Torr DCM; +, 10 Torr
DCM; , 23 Torr DCM; A, 50 Torr DCM;
x, 100 Torr DCM. (1 Torr = 1 mm Hg.)
The solutions were buffered to pH 7.4.
20
1
0.5
1.0
log pО2
1.5
2.0](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2F7e3218aa-1b65-42a2-9071-7edb43c3a555%2Fbb334896-9113-4335-8e0b-fe18f2086416%2F4gaon5s_processed.png&w=3840&q=75)
Transcribed Image Text:2. The diagram to the right shows the change in the
structure of the C-terminal portion of each of the ẞ-subu-
nits of human hemoglobin (HbA) in the oxyHb to deox-
yHb or R-to-T transition. The hydrogen bonding interac-
tion of the C-terminal ẞHis 146 residue with the side chain
of Asp94, highlighted by the red ellipse, has been shown
to be responsible for a major portion of the proton uptake
associated with the Bohr effect. Treatment of HbA with
the enzyme carboxypeptidase A (CPA) results in loss of
the C-terminal ẞHis 146 and ẞTyr145 residues of the ẞ-
subunits.
(a) ( ) Draw a Hill plot [log(Y/[1-Y]) vs. log(pO2), Y
= fraction of heme groups occupied by O2] to compare
the values of the Hill coefficient nн and the O2-binding
affinity at pH 7.4 of normal HbA before and after treat-
ment of with CPA.
(b) ('
) How will the plot for CPA-digested HbA
change at pH 7.2?
(c) 1
Hi5146
HN-
✓ Low PK
B-chain.
CH2
CH-NH-CO-CH-NH-
CH₂
Tyr145
он
HbO2
or R state
Туг145
CH-CH2-
OH
co
NH
CH
CH₂
His
Cy593
HS-CH=CH-NH-CO-
Co
NH
-CH-CH
Cy593
ASP94
HS-CR CH-NH-CO-
CO
N-H...O
NH
HN
-CH2-CH
High pk
Asp94
B-chain.
deoxyHb
or T state
Anesthetic gases used in surgery are known to bind to the hemoglobin molecule in red
blood cells. The diagram below illustrates O2 binding curves of normal human HbA in the presence of
the anesthetic gas dichloromethane (DCM).
% OXYGENATION
100
• UNTREATED
DCM 10 Torr
80
DCM 23 Torr
DCM 50 Torr
× DCM 100 Torr
60
40
Effect of dichloromethane (DCM) on
02 binding curves of HbA.
Symbols: O, 0 Torr DCM; +, 10 Torr
DCM; , 23 Torr DCM; A, 50 Torr DCM;
x, 100 Torr DCM. (1 Torr = 1 mm Hg.)
The solutions were buffered to pH 7.4.
20
1
0.5
1.0
log pО2
1.5
2.0
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