BCH 2333 Lecture Notes - Lecture 11: Protoporphyrin Ix, Dissociation Constant, Tautomer

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amberherring744

6 Apr 2016

School

University of Ottawa

Department

Biochemistry

Course

BCH 2333

Professor

Adam Jason Shuhendler

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Document Summary

Without oxygen transport proteins we would have a hundred fold less oxygen in our systems. Delivers oxygen to all the cells: myoglobin. First structure to have its crystal structure solved. They both bind oxygen with a prosthetic group. Prosthetic group is a non-protein molecule that is bound in the protein structure that help stabilize the final tertiary structure (low-energy); they provide the conformational lock that keeps the protein together. The two proteins bind reversible (transport mechanism). The structure of myoglobin is similar to a single subunit of hemoglobin. Ligand: is a small molecule that binds to a larger molecule. The heme structure (prosthesis) is called protoporphyrin ix (9)+fe2+ Myoglobin is a special case because it has an entropic gain, because it is highly hydrophobic on the inside, which allows it to interact with the protoporphyrin which is also very hydrophobic.

Related Questions

Match the words (A-E) with the statements below: ( 10 pts)

A. Bohr

B. 2, 3-BPG

C. Carbamate

D. Carbon dioxide

E. Concerted

F. Distal Histidine

G. Heme

H. Hemoglobin

I. Myoglobin

J. Sickle Cell Anemia

This has the ability to protect against carbon monoxide binding to the heme _______________

This is the molecule whose function is to facilitate diffusion of oxygen in muscle cells. ___________

The ability of myoglobin to bind oxygen depends on the presence of a bound prosthetic group called .

The shape of this protein has a sigmoidal curve _______________

As the partial pressure of ___________ increases, the affinity of oxygen binding to hemoglobin decreases. (there can be two answers)

The effect of hydrogen ions and carbon dioxide on the binding of oxygen to hemoglobin is called the _____________ effect

___________ is an allosteric effector that binds to the positive charges on the hemoglobin molecule .

Hemoglobin binding of oxygen is best described as a combination of sequential and ______________ model.

Carbon dioxide forms ______________ groups in proteins by reaction with N-terminal groups.

This condition is a result of a single-point mutation in the Î² chain of hemoglobin:__________________

BCH 2333 Lecture Notes - Lecture 11: Protoporphyrin Ix, Dissociation Constant, Tautomer

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