Please answer in full explaination The structure of the heme prosthetic group is shown. This group isplugged into the protein moiety of myoglobin as in the scheme below.Explain, which site of the heme structure, A or B, is this prosthetic groupplugged into the core moiety of the myoglobin globe?CH3-CH-CH₂CH₂HCCH₂CH3BCH₂CH₂N=CC-CH3CHCHC-CH3CH₂

Prosthetic groups are non amino acid components that are covalently linked to the protein. Heme…

Answered: The structure of the heme prosthetic…

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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Similar questions

The α and β subunits of hemoglobin bear a remarkable structural similarity to myoglobin. However, in the subunits of hemoglobin, certain residues that are hydrophilic in myoglobin are hydrophobic. Why might this be the case?
Identify the incorrect statement regarding the polypeptide, Myoglobin. Select one: a. The interaction between Myoglobin and O2 is homotopic in nature as indicated by a Hill coefficient n = : 1 b. Myoglobin is found predominantly in muscle tissue because it facilitates oxygen diffusion. c. The majority of Myoglobin's secondary structure is composed of alpha-helices d. Myoglobin has a higher affinity for oxygen than Hemoglobin e. Myoglobin serves as an oxygen storage protein as suggested by its hyperbolic binding of 02
Myoglobin monomers are likely to have more hydrophilic amino acids on the protein surface than Hemoglobin monomers. True or False
The primary and tertiary structures of hemoglobin and myoglobin are very similar and both contain the 'heme' group as an oxygen-binding prosthetic group. However this There are important functional differences between the two proteins. Hemoglobin oxygen transport protein, myoglobin functions as oxygen storage protein. Hemoglobin and consider the structural differences and oxygen binding curves between myoglobin why myoglobin is a good oxygen transport protein, while hemoglobin Explain why it cannot be a good oxygen storage protein.
The subunits of hemoglobin and myoglobin share structural similarities. Some residues are hydrophilic in hemoglobin but are hydrophilic in myoglobin. Give an explanation as to why this may be the case.
The following sequence of amino acids are part of adult hemoglobin from the N-terminus. DRAW THE STRUCTURE OF THIS PEPTIDE. Val-His-Leu-Thr-Pro-Glu-Glu-Lys-Ser-Ala-Val-Thr
Myoglobin stores O2 in muscle tissue to be used by the mitochondria only when the cell is in oxygen debt, whereas hemoglobin can effectively transport O2 from the lungs and deliver it discriminately to cells in need of O2. Describe the structural features that allow these two proteins to accomplish separate functions.
Calculate the percent oxygen saturation of myoglobin if 7 of 15 binding sites are occupied..
Apohemoglobin (apoHb) is a dimeric globular protein with two vacant heme‐binding. The preparationof apoHb is based on partial hemoglobin (Hb) unfolding to facilitate heme extraction into an organic solvent. What is an appropriate method for removing the heme? a. An acidic buffer to protonate the His axial ligand in the presence of ureaas the denaturing agent. b. An acidic buffer to protonate the His axial ligand in the presence of mercatoethanol as the denaturing agent. c. A basic buffer to deprotonate the His axial ligand in the presence of ureaas the denaturing agent. d. An basic buffer to protonate the His axial ligand in the presence of mercatoethanol as the denaturing agent.
In some metalloproteins such as haemoglobin and some metalloenzymes, the Fe2+ metal is not bound to the amino acid side-chains of the protien,but to a prophrin ring called a heme prosthetic group. How does the heme coordinate to the iron?
I now know the structure difference between myoglobin and hemoglobin , however which exctaly structure difference make myglobin become a oxygen storage ? and not a oxygen transport?? Be specific! details describe how the structure connect to their role. also which exctaly structure difference make hemoglobin become better oxygen transport?? I need the specific structure that contribute to their unique role. I KNOW THE STRUCTURE DIFFERENCE , but don't understand which specific part make myoglobin only bind to oxygen, and not release oxygen
What is one feature of fibrillar collagen that contributes to its strength? They form crosslinks between glycine and alanine residues on adjacent collagens. They form crosslinks between lysine and hydroxylysine residues on one collagen molecule. They form crosslinks between glycine and alanine residues on one collagen molecule. They form crosslinks between lysine and hydroxylysine residues on adjacent collagen molecules.

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