please answer #3 34a.b.Name and very briefly describe the four levels of protein structure.Hemoglobin has a quaternary structure known as a2ß2 What would be thequaternary structure of a protein having four polypeptides that are alldifferent?Below is the chemical equation for O2 binding to myoglobin (Mb).Mb-02O2 + Mb

As per the central dogma of molecular biology, DNA contains the code that is necessary for the…

Answered: 3 a. b. Name and very briefly describe…

Biology: The Dynamic Science (MindTap Course List)

4th Edition

ISBN:9781305389892

Author:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Publisher:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Chapter47: Animal Nutrition

Section: Chapter Questions

Problem 13TYK

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Describe the differences in the four protein structures.
Describe the effect of the amino acid change on protein function: how does the HbS protein function differently than the HbA protein in red blood cells?
List 4 different actiated carrier molecules, for each one, list both the oxided and reduced forms
1. What is hemoglobinopathy? What is sickle-cell anemia? Explain the concept relating to protein structure. 2. How does the oxygen-carrying functions of myoglobin differ from that of hemoglobin?
q41 please calculate the unknown concentration of the protein D wih an absorbance value of A412 given the standard curve indicated in the table. write your answers in numbers only with 2 decimals. protein concentration (ug/ml) absorbance 0 0.000 0.02 0.161 0.04 0.284 0.06 0.438 0.08 0.572 0.10 0.762
Which intermolecular forces are important in acetic acid, CH3 –(C=0)-oh? A particular amino acid contains a- CHNH3+ group. Is this amino acid more likely to be found on the inside or the outside of the folded protein? Briefly explain. The addition of ethanol, CH3CHOH, t an aqueous solution lowers the surface tension of the solution. Predict whether adding ethanol to an aqueous protein solution will tend to stabilize or unfold the protein. Briefly explain.
a. Why proteins are extracted to a buffered solution? Briefly describe the components of ageneralized protein extraction buffer?.b. Describe the basis of affinity chromatography in protein purification.c. What is the most appropriate method of protein elution in affinity chromatography?d. List three examples of commonly employed combinations of ligand and protein in affinitychromatography.
Normal Hgb is referred to as HbA and contains 4 subunits, 2 α-globin chains and 2 β-globin chains, arranged as two dimers of αβ. In Sickle Cell Disease, both β-globin chains are altered in the dimers (αβS/αβS). Q3: Which level of structure does the αβ/αβ and αβS/αβS in HbA and HbS describe?
Many plasma proteins found in an aqueous environment are globular in shape. Which amino acid side chains would you expect to find on the surface of a globular protein and in contact with the aqueous environment? Which would you expect to find inside, shielded from the aqueous environment? Explain. Q.) Arg
1. In a protein, why does when Ala is replaced with Ile, it loses its activity but when Lys is replaced by Arg and Leu to Ile, it only has little effect on protein structure and function? Explain. 2. Why do proteins cannot be denatured reversibly when they are chemically altered to change the chemical composition of certain side chains? Explain.
In a molecular disease of hemoglobin, Hemoglobin Rainier, Tyr 145β is replaced by Cys, which forms a disulfide bond with another Cysresidue in the same subunit. This prevents the formation of ion pairs that normally stabilize the T state. How does hemoglobin Rainier differ from normal hemoglobin with respect to the Hillcoefficient? Explain your answers.
what are the structural features of the protein 6VJI? primary , secondary What are two features of 6VJI's What are two features of your protein’s structure that make it different or similar to haemoglobin are two features of your protein’s structure that make it different or similar to haemoglobin? structure that make it different or similar to haemoglobin?

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3 a. b. Name and very briefly describe the four levels of protein structure. Hemoglobin has a quaternary structure known as a2ß2 What would be the quaternary structure of a protein having four polypeptides that are all different?