Protein Conformations Overview

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Questions and Answers

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?

<p>Intrinsically disordered segments (B)</p> Signup and view all the answers

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

<p>When they have the lowest free energy (C)</p> Signup and view all the answers

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

<p>15 to 80 kJ/mol (A)</p> Signup and view all the answers

Where are disulfide bonds primarily found in eukaryotes?

<p>In secreted, extracellular proteins (B)</p> Signup and view all the answers

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

<p>Thermophilic bacteria and archaea (B)</p> Signup and view all the answers

What type of interactions primarily stabilize protein structure?

<p>Weak interactions (C)</p> Signup and view all the answers

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

<p>Extracellular space (C)</p> Signup and view all the answers

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

<p>Weak interactions are much weaker than individual covalent bonds (B)</p> Signup and view all the answers

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