Protease Mechanisms 1

Protease Mechanisms 1

Assessment

Interactive Video

Science, Chemistry

University

Hard

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The video tutorial provides an in-depth understanding of proteases, focusing on their structure, types, and mechanisms. It explains the differences between serine and cysteine proteases, with a particular emphasis on caspases, which are cysteine proteases involved in apoptosis. The tutorial also covers the identification of peptide bonds targeted by proteases and the role of active sites in enzyme function.

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10 questions

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1.

MULTIPLE CHOICE QUESTION

30 sec • 1 pt

What are the two main types of proteases discussed in the video?

Lysine and arginine proteases

N-terminal and C-terminal proteases

Serine and cysteine proteases

Aspartate and glutamate proteases

2.

MULTIPLE CHOICE QUESTION

30 sec • 1 pt

What is the primary target of caspases in a protein chain?

Aspartate residues

Tyrosine residues

Tryptophan residues

Phenylalanine residues

3.

MULTIPLE CHOICE QUESTION

30 sec • 1 pt

Why is it important to identify the alpha carbon in a protein chain?

To predict the protein's folding pattern

To identify the site of protease action

To understand the protein's solubility

To determine the protein's molecular weight

4.

MULTIPLE CHOICE QUESTION

30 sec • 1 pt

What role does histidine play in the active site of cysteine proteases?

It acts as a nucleophile

It stabilizes the protein structure

It abstracts a proton from the sulfhydryl group

It binds to the substrate

5.

MULTIPLE CHOICE QUESTION

30 sec • 1 pt

Which element is part of the serine residue that makes it similar to cysteine?

Nitrogen

Carbon

Oxygen

Sulfur

6.

MULTIPLE CHOICE QUESTION

30 sec • 1 pt

What is the main difference between serine and cysteine proteases?

The type of nucleophile they use

The size of their active site

The type of substrate they bind

The pH at which they operate

7.

MULTIPLE CHOICE QUESTION

30 sec • 1 pt

What is the function of the hydrogen bond in the active site of proteases?

To provide energy for the reaction

To hold the histidine in a specific orientation

To increase the enzyme's solubility

To bind the substrate tightly

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