Table of contents

1. Introduction to Biochemistry4h 34m
2. Water3h 23m
3. Amino Acids8h 10m
4. Protein Structure10h 4m
5. Protein Techniques14h 5m
6. Enzymes and Enzyme Kinetics13h 38m
7. Enzyme Inhibition and Regulation 8h 42m
8. Protein Function 9h 41m
9. Carbohydrates7h 49m
10. Lipids5h 49m
11. Biological Membranes and Transport 6h 37m
12. Biosignaling9h 45m
Review 1: Nucleic Acids, Lipids, & Membranes2h 47m
Review 2: Biosignaling, Glycolysis, Gluconeogenesis, & PP-Pathway3h 12m
Review 3: Pyruvate & Fatty Acid Oxidation, Citric Acid Cycle, & Glycogen Metabolism2h 26m
Review 4: Amino Acid Oxidation, Oxidative Phosphorylation, & Photophosphorylation1h 48m

8. Protein Function

Motor Proteins

Biochemistry

8. Protein Function

Motor Proteins

Previous problemNext problem

Struggling with Biochemistry?

Join thousands of students who trust us to help them ace their exams!Watch the first video

Multiple Choice

What are the common features of the motor proteins kinesin and dynein?

Both types of motor proteins bind microtubules.

Both types of motor proteins bind and hydrolyze ATP.

Both types of motor proteins undergo conformational changes when they travel along the microtubule.

Both types of motor proteins 'step' from one tubulin subunit to another.

All of the above are true.

Previous problemNext problem

Verified step by step guidance

Understand that motor proteins are molecular machines that convert chemical energy into mechanical work, allowing them to move along cytoskeletal filaments.

Recognize that kinesin and dynein are two types of motor proteins that specifically interact with microtubules, which are part of the cytoskeleton.

Both kinesin and dynein bind to microtubules, which are composed of tubulin subunits, allowing them to transport cellular cargo along these structures.

Both motor proteins utilize ATP as an energy source. They bind and hydrolyze ATP, which provides the energy required for their movement along the microtubules.

During their movement, both kinesin and dynein undergo conformational changes, which are structural changes that occur in the protein, enabling them to 'step' from one tubulin subunit to another, effectively moving along the microtubule.