8.Structure and functions of oligomeric proteins.Hemoglobin: structure, oxygen saturation curve, transport ofoxygen, agents affecting oxygen binding.9 Cofactors of enzymes CoenzymesVitamins as coenzymes

The production, growth, and differentiation of all types of blood cells are referred to as…

Answered: 8.Structure and functions of oligomeric…

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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17. Muscle. Contractions which move the body depend heavily on diffusion. Why do we have difficulty moving our fingers etc. when they are cold ?
Dr. Jill, a competitive researcher, aims to win a University Research Grant. She wanted to investigate the role of hemoglobin in oxygen transport. To know more about the protein, she decided to use the Protein Data Bank (PDB) deposited information of 3HRW, a hemoglobin from mouse (Mus musculus). Support Dr. Jill in the exciting part of her research by answering the following questions How many amino acid residues comprise the protein? ______________ The hemoglobin from Mus musculus is classified under what group of enzymes? ______________ What experimental method was used to determine the structure? ______________ Under Domain Annotation by SCOP, how many chains comprise this enzyme? ______________ What is the superfamily of proteins in which hemoglobin is categorized?______________
6. Quaternary structure. Oligomeric and polymeric proteins. Formation of a quaternary structure of proteins from several domains. Chemical bonds that form and stabilize a given structure.
Part 1: For the following statement choose (T) for true and (F) for fal 1. Animals can synthesize proteins from inorganic N present in the air. 2. Proteins have higher molecular mass than carbohydrates and lipids 3. When 2 amino acids combine, the product is called a dipeptide. 4. The structure of human insulin is example of tertiary structure of 5. Hemoglobin is example of a quaternary structure. 6. Enzymes decreases the speed of a reaction 7. Nearly all enzymes are globular proteins. 3. Optimum temperature of the enzyme, is 37°C or body tempera . Vitamins are synthesized in the body. J. vitamin deficiency can generate a number of diseases.
(schematically) these structures. 4. Principles of domain organization of protein structure. Structural and functional domains. Determination of domains in protein folding.
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
Which of the following is a primary function of molecule b ?
10
Describe the reason why the red blood cells placed in one solution swell and burst and also why the red blood cells placed in another solution shrink and wrinkle.
describe hemoglobin is a protein composed of four polypeptide chains
4/ Which of the following is true for all proteins? Select the correct response(s): • They are the predominant biomolecular component of the cells. They are water soluble in nature. They are acidic in nature. They are neutral in net charge. They are polymers of amino acids. They are globular in shape. They are the primary source of energy of the body.

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8.Structure and functions of oligomeric proteins. Hemoglobin: structure, oxygen saturation curve, transport of oxygen, agents affecting oxygen binding.