Protein Conformations Overview

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What does a change in conformation of a protein involve?

Disruption of hydrogen bonds

Formation of new bonds

Rotation about single bonds (correct)

Breaking covalent bonds

Why do proteins need to adopt multiple stable conformations?

To increase the number of hydrogen bonds

To facilitate binding to other molecules or catalyze reactions (correct)

To decrease the thermodynamic stability

To break covalent bonds efficiently

What term is used to describe proteins in their functional, folded conformations?

Denatured proteins

Native proteins (correct)

Non-native proteins

Partially folded proteins

What are protein segments that lack discernible structure referred to as?

Intrinsically disordered segments Signup and view all the answers

Under what conditions do the existing protein conformations tend to be the most stable?

When they have the lowest free energy Signup and view all the answers

What is the range of ΔG separating the folded and unfolded states in typical proteins under physiological conditions?

15 to 80 kJ/mol Signup and view all the answers

Where are disulfide bonds primarily found in eukaryotes?

In secreted, extracellular proteins Signup and view all the answers

Which type of bacteria typically have many proteins with stabilizing disulfide bonds?

Thermophilic bacteria and archaea Signup and view all the answers

What type of interactions primarily stabilize protein structure?

Weak interactions Signup and view all the answers

In which part of a typical cell is the environment more likely to support disulfide bond formation?

Extracellular space Signup and view all the answers

How do weak interactions compare to individual covalent bonds in terms of breaking strength?

Weak interactions are much weaker than individual covalent bonds Signup and view all the answers

Protein Conformations Overview

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Questions and Answers

What does a change in conformation of a protein involve?

Why do proteins need to adopt multiple stable conformations?

What term is used to describe proteins in their functional, folded conformations?

What are protein segments that lack discernible structure referred to as?

Under what conditions do the existing protein conformations tend to be the most stable?

What is the range of ΔG separating the folded and unfolded states in typical proteins under physiological conditions?

Where are disulfide bonds primarily found in eukaryotes?

Which type of bacteria typically have many proteins with stabilizing disulfide bonds?

What type of interactions primarily stabilize protein structure?

In which part of a typical cell is the environment more likely to support disulfide bond formation?

How do weak interactions compare to individual covalent bonds in terms of breaking strength?

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