Hemoglobin Function and Binding Dynamics

Hemoglobin Function and Binding Dynamics

Assessment

Interactive Video

Biology, Science, Chemistry

11th - 12th Grade

Practice Problem

Hard

Created by

Patricia Brown

FREE Resource

The video lecture discusses the oxygen-hemoglobin dissociation curve, explaining the structure of hemoglobin and its role in oxygen transport. It covers glycolysis as the energy source for red blood cells and introduces the concept of cooperativity in hemoglobin binding. The Haldane effect is explained, highlighting the release of CO2 when oxygen binds to hemoglobin. The lecture also explores factors that shift the hemoglobin binding curve, such as pH, temperature, and 2,3-BPG, and their implications for oxygen delivery in different physiological conditions.

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10 questions

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1.

MULTIPLE CHOICE QUESTION

30 sec • 1 pt

What is the primary source of energy for red blood cells?

Photosynthesis

Glycolysis

Fermentation

Oxidative phosphorylation

2.

MULTIPLE CHOICE QUESTION

30 sec • 1 pt

How many subunits does a hemoglobin molecule have?

Three

Two

Four

Five

3.

MULTIPLE CHOICE QUESTION

30 sec • 1 pt

What is the term used to describe the increased affinity for oxygen binding after the first oxygen molecule binds to hemoglobin?

Cooperativity

Competition

Inhibition

Saturation

4.

MULTIPLE CHOICE QUESTION

30 sec • 1 pt

What happens to carbon dioxide when oxygen binds to hemoglobin?

It is absorbed

It is released

It forms carbonic acid

It remains unchanged

5.

MULTIPLE CHOICE QUESTION

30 sec • 1 pt

What does a rightward shift in the hemoglobin binding curve indicate?

No change in oxygen affinity

Increased oxygen affinity

Increased carbon dioxide binding

Decreased oxygen affinity

6.

MULTIPLE CHOICE QUESTION

30 sec • 1 pt

Which condition is likely to cause a rightward shift in the hemoglobin binding curve?

Low 2,3-BPG levels

Low temperature

High pH

High carbon dioxide levels

7.

MULTIPLE CHOICE QUESTION

30 sec • 1 pt

What is the role of 2,3-BPG in oxygen release from hemoglobin?

It decreases oxygen affinity

It increases oxygen affinity

It has no effect

It binds to oxygen directly

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