help. 2. The following graph illustrate the binding of 02 to proteins: myoglobin andhemoglobin ( one curve is for myoglobin, the other for hemoglobin)1.0 r0.8O 0.60.40.20.0004080120Po,, mm Hga. Assign the curves to it corresponding proteins by labeling them with thecorresponding protein names on the figureb. Estimate the Ps0 (similar to Kd) for each of the proteins, Illustrating yourestimation process by drawing line on the figures.

Hemoglobin is an oligomeric conjugated protein with four peptide chains joined by a…

Answered: 2. The following graph illustrate the…

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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The figure below shows amino acid interactions between the a /B2 subunit interface of hemoglobin. These interactions stabilize the T state of the protein. Based on the figure below, which amino acid in the picture below, if replaced with glutamate, would decrease the Ka of hemoglobin for O2 the most? Include both the residue and the residue number in your response (For example, V1 or K127). to B, V34 8- a, R141 D126 K127 Noncovalent
The figure below shows amino acid interactions between the a1/B2 subunit interface of hemoglobin. These interactions stabilize the T state of the protein. Based on the figure below, which amino acid in the picture below, if replaced with glutamate, would decrease the Kg of hemoglobin for O2 the most? Include both the residue and the residue number in your response (For example, V1 or K127). B, V34 8- a, R141 a2 D126 a, K127 Noncovalent Interactions
1. The human hemoglobin molecule, like all mammalian he- moglobins, is comprised of two a-chains and two ß-chains con- ₂ taining 141 and 146 amino acid residues, respectively. Be- cause the molecule possesses two-fold symmetry, there are a1-a2, B1-B2, and a1-B2 interfaces formed by amino acid sidechains through which structural changes are transmitted underlying ligand binding. The most important of these is the a1-B2 interface that is illustrated in the diagram on the right. All of the sidechain interactions across the a1-B2 interface are hydrophobic except for that between Asp(a94) and Asn- (B102). This is the only polar interaction across the α1-³2 in- terface and it helps to stabilize the oxy- or R-conformation. Its approximate location in the Hb molecule is represented by the red double arrow in the diagram on the right. His FG4 97 Asp G1 (99) Tyr C7 (42) Hb mutant (a) T State (deoxy) 95 The C6 41 (a) The diagram below on the right-hand side illustrates the polar Asp(a94). . . Asn…
Please fill in the following blanks with the options that correctly finishes the sentence. a. At a low O₂ pressure the [Select] hemoglobin is in a [Select] [Select] [Select] 9 [Select] " bond with [Select] heme, and the protein's central channel is [Select] b. The proximal histidine forms a(n) [Select] state is stabilized. In this conformation state, the heme prosthetic groups is each subunit's heme is more likely to be the proximal histidine is [Select ] bond with while the distal histidine forms a(n) [Select] to the
PLEASE MAKE THE DR BRUJIN GRAPH From these k-mers construct a de Bruijn graph and determine the sequence of the contig. AGCG ATCT ATGA ATGG ATTC CCCT CCTG CTCT CTGA CTGC CTTT GAAG GATT GCGT GCTC GTTC TATG TCAT TCTA TCTT TGAA TGAT TGGA TGTT TTCA TTCC TTTC
= A different Fab fragment binds to lysozyme with a dissociation constant of Ka 10-6 M. A 1 nM (10-9 M) solution of lysozyme is treated with increasing concentrations of this Fab fragment. At what concentration of added Fab will half of the lysozyme be bound to this Fab? [F] = ab M
The graphs below show 02-binding curves of several proteins including myoglobin (Mb) and hemoglobin (Hb). If curve 3 (-) represents the 02 binding behavior of normal hemoglobin, which curve represents an 02-binding transporter with the same p50 as normal hemoglobin? 1.0- YO, 0.5 0.0 pO,(torr) O A. 1 B. 2 O C. 4 O D. 5 E. Both "2" and "4"
for the next 7 items, refer to the figure below: 2 6 Asn - Cyst - Pro Leu Gly - NH; 3 4 8 Cyst - Tyr - Ille Oxytocin (Human) Gln 2 Phe - Gln Asn - Cyst - Pro - Arg - Gly - NH: Cyst - Tyr Arginine Vasopressin (Human) 4. These molecules are: A. proteins B. nonapeptide C. polypeptide D. amino peptide _5. What is the classification of these molecules based on function? C. hormones A. Structural proteins B. antibody D. enzyme 6. What is the classification of these molecules based on composition? A. pure B. simple C. conjugated D. compound _7. What is the classification of these molecules based on composition? C. conjugated D. compound A. pure B. simple What chemical bond/sis/are present in these peptides? A. peptide bond only B. disulfide bond only _8. C. peptide bonds and disulfide bonds D. glycosidic bond _9. Which of these peptides contain an amino acid with a side chain IMIDAZOLE? C. Hard to tell А. Охytocin B. Vasopressin D. Either A or B Based on amino acid composition, what is the…
2B. S. aureus hemolysin B attacks the RBC cell membrane by hydrolyzing the sphingomyelin headgroup: ОН HN .R hemolysin B cuts this bond i) Draw a plausible mechanism of hydrolysis for this lipid headgroup. Let B- and BH be general base and general acid. 00-P-O LOR2 OR, ii) Why is this damaging to the overall membrane architecture of the RBC?
The figure shows interaction of various amino acids (Phe, Arg, and Asn) present in Hb with 2,3-DPG. The side chains of these amino acids and 2,3-DPG interactions are circled in red. HO Но Phe HN Asn H2N NH Arg You identify a mutant version of the globin chain where the Arg in circle 2 is replaced with aspartic acid in a patient. Would the Hb protein in this patient be able to transport oxygen even in the presence of 2,3-DPG? ASPARTIC ACID (asp) No, because the mutant Hb version will bind 2,3 DPG, and not oxygen Yes, because the mutant Hb version will bind 2,3 DPG, and not oxygen Yes, because the mutant Hb version will bind oxygen and not 2,3 DPG
Why does the dissociation constant change for hemoglobin in high and low 02 concentrations? O Hemoglobin is a tetramer and subunits have decreased dissociation of 02 when a neighboring subunit has bound 02 O Hemoglobin is a monomeric protein with increased dissociation of 02 when a neighboring molecule has bound 02 O Hemoglobin is a tetramer and subunits have increased dissociation of 02 when a neighboring subunit has bound CO O Hemoglobin is a tetramer and subunits have increased dissociation of O2 when a neighboring subunit has bound O2
The T state of hemoglobin is converted to the R state by what event? Select one: The binding of oxygen destabilizes a more planar heme ring which alters the position of the proximal histidine and subsequently, residues between the alß2 interface. а. b. None of these. The binding of oxygen stabilizes a more planar heme ring which alters the position of the proximal proline and subsequently, residues between the alß2 interface. С. d. The binding of oxygen stabilizes a more planar heme ring which alters the position of the proximal histidine and subsequently, residues between the alß2 interface. The binding of oxygen destabilizes a more planar heme ring which alters the position of the proximal proline and subsequently, residues between the alß2 interface. е.

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