35 Questions
In protein folding, what does Phi represent?
N-C⍺ bond
Which type of bond is associated with Psi in protein folding?
C⍺-C bond
What is the primary reason behind the energy barrier in protein folding?
Steric hindrance
Which term describes the fully extended conformation of a polypeptide chain?
Main chain
What type of interaction drives hydrophobic amino acids to cluster together during protein folding?
Van der Waals interactions
Which model suggests that proteins fold into their native structure due to minimal free energy states?
Anfinsen's thermodynamic hypothesis
Which type of interaction is critical for stabilizing the secondary structure of proteins?
Hydrogen bonds
In protein folding, what is the primary role of chaperone proteins?
Assisting in correct folding of proteins
Which component of an amino acid residue contributes most to the hydrophobic effect in protein folding?
R-group/side chain
What is the major consequence of Misfolded proteins on cellular function?
Disruption of normal cellular processes
In protein folding, what angle is nearly always negative except in a left-hand helix?
Phi
Which amino acid has a planar (flat) structure when viewed side-on, with the R-group CH3 facing forward?
Alanine
What type of structure does the peptide bond exhibit in terms of rotation?
It cannot rotate
According to the Anfinsen hypothesis, which protein folding model involves a diverse population of structures with no structure preference?
Unfolded
What type of movement characterizes protein folding in terms of thermodynamics?
Movement from disorder to order
Which angle associated with the peptide bond can be both positive or negative?
Psi
What is the term used to describe the movement of protein folding from a high energy state to a lower energy state?
Energy funneling
Which amino acid's R-group contains a CH3 group and exhibits a planar structure?
Alanine
What is the primary movement described in protein folding based on thermodynamic principles?
Movement towards a lower energy state
In which model of protein folding does the native structure represent one stable conformation?
2 state model
Which interaction is the largest driver of protein folding?
Hydrophobic effect
In protein folding, what does the term 'unfolded state' refer to?
A state with a diverse population of structures
What does a 2-state model of protein folding suggest?
Proteins can exist in only two conformations: folded and unfolded
What is the thermodynamic driving force for protein folding?
Decrease in Gibbs free energy
How many different conformers can be formed in a 100 amino acid protein based on phi and psi bond angles?
$10^{30}$
Which type of interactions are primarily responsible for maintaining the native structure of proteins?
Hydrophobic interactions
'Folding is thermodynamically driven' implies that:
Folding always results in a lower energy state
'Delta G = Delta H - T Delta S' represents the relationship between which variables?
$\Delta G$, enthalpy, temperature, entropy
'50% of molecules unfolded and 50% of molecules still folded' refers to which point in protein folding?
$T = 0.5$ fraction unfolded point
'At midpoint 50% of the molecular population still knows how to fold' implies what about the folding process?
'Knowing how to fold' refers to a structural memory in proteins
What is the primary driving force behind the hydrophobic effect in protein folding?
Hydrophobic interactions
Describe the process of protein unfolding and its impact on the native conformation.
Protein unfolding disrupts the native structure, leading to loss of function and potential aggregation.
What defines the native conformation of a protein?
The stable, biologically functional structure adopted by a protein.
Explain the importance of tertiary structure in protein folding.
Tertiary structure determines the final 3D shape of a protein, essential for its function.
How does the hydrophobic effect contribute to stabilizing the tertiary structure of proteins?
Hydrophobic amino acids bury within the protein core, minimizing contact with water.
Test your knowledge on protein folding and the geometry associated with peptide bonds. Learn about the constraints on psi/phi angles and rotations around the peptide bond. This quiz references content from Mark Carlile's work.
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