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Oxygen Delivery and Protein Folding: Hemoglobin and Urea Denaturation, Assignments of Biochemistry

Two key topics in biochemistry: oxygen delivery by hemoglobin and protein folding. It delves into the mechanisms by which carbon dioxide (co2) affects the oxygen binding properties of hemoglobin, a crucial protein responsible for transporting oxygen to tissues and removing co2. The document also examines how the chemical structure of urea can disrupt the hydrogen bonding between amino acids, leading to the denaturation of proteins during gel electrophoresis analysis. Detailed explanations and illustrations to help understand these fundamental concepts in biochemistry. By studying this document, students can gain insights into the complex regulatory mechanisms of hemoglobin, the importance of protein structure and folding, and the practical applications of these principles in biochemical techniques like gel electrophoresis.

Typology: Assignments

2023/2024

Uploaded on 03/27/2024

kidus-yohannes
kidus-yohannes 🇺🇸

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5. Oxygen Delivery: Hemoglobin is a remarkable protein that is responsible not only for the
delivery of oxygen to tissues, but also the removal of CO2. Due to the unique function of
this protein it is highly regulated to be sensitive to environmental conditions. A primary
effector of O2 binding is CO2, which is able to affect hemoglobin via two different
mechanisms.
a) One mechanism is via allosteric binding to the amino terminal of the a subunit. The binding
affects the overall structure of the protein and alters the oxygen binding curve. Draw the
reaction of the amino terminus (hint: treat the amine as an NH2 nucleophile) with CO2 to
produce a carbamate and a proton.
b) Using the equilibrium expression for allosteric effectors presented in class to sketch a rough
oxygen binding curve a) under normal conditions and b) under elevated CO2 conditions.
R-NH2
+
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5. Oxygen Delivery : Hemoglobin is a remarkable protein that is responsible not only for the delivery of oxygen to tissues, but also the removal of CO 2. Due to the unique function of this protein it is highly regulated to be sensitive to environmental conditions. A primary effector of O 2 binding is CO 2 , which is able to affect hemoglobin via two different mechanisms. a) One mechanism is via allosteric binding to the amino terminal of the a subunit. The binding affects the overall structure of the protein and alters the oxygen binding curve. Draw the reaction of the amino terminus (hint: treat the amine as an – NH 2 nucleophile) with CO 2 to produce a carbamate and a proton. b) Using the equilibrium expression for allosteric effectors presented in class to sketch a rough oxygen binding curve a) under normal conditions and b) under elevated CO 2 conditions.

R-NH2+^ (^

  • p. *

-Go

tHT

ideation. o elevation

POz

  1. Protein folding: In order to analyze proteins via gel electrophoresis they are typically denatured using urea. Using the chemical structure of urea and the two amino acids draw a scheme depicting how it can disrupt hydrogen bonding between a lysine nitrogen and the carbonyl oxygen of glutamine. Draw a squiggly line for the protein backbone and the actual chemical structures of the Lys and Gln R groups interacting. Lys + Gln w/ H-bond Lys Urea and Gln + Urea (disrupted H-bond)
NH

.. f WH &

H-bond
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I

④ -^ CH^
  • CH2-CH2-CH2-Nyt
  • CH2-CH2-CH2-N-H ..... HN^

o fH bond

d

H-bond
  • NH -^ : CHICHz"C
  • (^) NH

-CH2-tHa-k/

H-bond

NE

NH