Podcast
Questions and Answers
What term was first coined in 1983 by A. Wada and M. Ohgushi?
What term was first coined in 1983 by A. Wada and M. Ohgushi?
- Intrinsically unstructured protein
- Molecular chaperone
- Molten globule (correct)
- Denatured protein
Under what conditions was the molten globule first found in cytochrome c?
Under what conditions was the molten globule first found in cytochrome c?
- High pH and low salt concentration
- Neutral pH and moderate salt concentration
- Low pH and low salt concentration
- Low pH and high salt concentration (correct)
Which type of proteins lack a well-structured three-dimensional fold?
Which type of proteins lack a well-structured three-dimensional fold?
- Intrinsically unstructured proteins (correct)
- Fibrous proteins
- Membrane proteins
- Globular proteins
What is the function of molecular chaperones in protein folding?
What is the function of molecular chaperones in protein folding?
Which phenomenon describes the tendency of nonpolar molecules to aggregate in an aqueous environment?
Which phenomenon describes the tendency of nonpolar molecules to aggregate in an aqueous environment?
What type of interactions are involved in the tertiary structure of proteins?
What type of interactions are involved in the tertiary structure of proteins?
Which protein exhibits cooperativity in oxygen binding?
Which protein exhibits cooperativity in oxygen binding?
What is the primary structural component of hair and wool?
What is the primary structural component of hair and wool?
Which protein is found in muscle and tissue and binds only one oxygen molecule?
Which protein is found in muscle and tissue and binds only one oxygen molecule?
Proper protein folding is essential for the creation of which protein structure?
Proper protein folding is essential for the creation of which protein structure?
What is the name of the Google AI offshoot that developed the AI network for protein structure prediction?
What is the name of the Google AI offshoot that developed the AI network for protein structure prediction?
Which yearly protein structure prediction challenge did AlphaFold win?
Which yearly protein structure prediction challenge did AlphaFold win?
Who co-founded CASP in 1994 to improve computational methods for predicting protein structures?
Who co-founded CASP in 1994 to improve computational methods for predicting protein structures?
Which term refers to determining a protein’s 3D shape from its amino-acid sequence?
Which term refers to determining a protein’s 3D shape from its amino-acid sequence?
What is the name of the biennial protein structure prediction challenge that AlphaFold participated in?
What is the name of the biennial protein structure prediction challenge that AlphaFold participated in?
What is denaturation in the context of proteins?
What is denaturation in the context of proteins?
Which of the following can cause denaturation of proteins?
Which of the following can cause denaturation of proteins?
What is the role of molecular chaperones in protein folding?
What is the role of molecular chaperones in protein folding?
How do membrane proteins differ from globular proteins in terms of hydrophobic residues?
How do membrane proteins differ from globular proteins in terms of hydrophobic residues?
What effect does the hydrophobic effect have on proteins in water?
What effect does the hydrophobic effect have on proteins in water?
What is the main characteristic of globular proteins?
What is the main characteristic of globular proteins?
Which statement best describes the tertiary (3°) structure of proteins?
Which statement best describes the tertiary (3°) structure of proteins?
What is a common characteristic of fibrous proteins?
What is a common characteristic of fibrous proteins?
Which type of protein structure contains polypeptide chains organized approximately parallel along a single axis?
Which type of protein structure contains polypeptide chains organized approximately parallel along a single axis?
What type of proteins are often approximated as spheres, tend to be water-soluble, and have polar residues on the exterior?
What type of proteins are often approximated as spheres, tend to be water-soluble, and have polar residues on the exterior?
Which term refers to the sequence of amino acids in a polypeptide chain?
Which term refers to the sequence of amino acids in a polypeptide chain?
What type of bonds are primarily responsible for maintaining local conformations in secondary protein structures?
What type of bonds are primarily responsible for maintaining local conformations in secondary protein structures?
Which of the following is NOT a type of secondary protein structure?
Which of the following is NOT a type of secondary protein structure?
In an α-helix, how is the C=O of one amino acid oriented with respect to the N-H of an amino acid four residues down the chain?
In an α-helix, how is the C=O of one amino acid oriented with respect to the N-H of an amino acid four residues down the chain?
Which type of interaction is primarily responsible for the hydrophobic effect in protein folding?
Which type of interaction is primarily responsible for the hydrophobic effect in protein folding?
What causes a bend in an alpha helix structure?
What causes a bend in an alpha helix structure?
Which amino acid is known to disrupt the alpha helix structure?
Which amino acid is known to disrupt the alpha helix structure?
What is the distance for one turn in an alpha helix structure?
What is the distance for one turn in an alpha helix structure?
In beta-pleated sheets, hydrogen bonds form between the backbone of which component?
In beta-pleated sheets, hydrogen bonds form between the backbone of which component?
Which structural element causes steric crowding in an alpha helix?
Which structural element causes steric crowding in an alpha helix?
What type of turn involves Glycine in protein structure?
What type of turn involves Glycine in protein structure?
What disrupts the alpha-helix structure due to strong electrostatic repulsion?
What disrupts the alpha-helix structure due to strong electrostatic repulsion?
What is a major factor contributing to the denaturation of proteins?
What is a major factor contributing to the denaturation of proteins?
Which type of protein structure prediction challenge did AlphaFold win?
Which type of protein structure prediction challenge did AlphaFold win?
In protein folding, what is the role of molecular chaperones?
In protein folding, what is the role of molecular chaperones?
What distinguishes membrane proteins from globular proteins in terms of hydrophobic residues?
What distinguishes membrane proteins from globular proteins in terms of hydrophobic residues?
What effect does the hydrophobic effect have on protein folding in aqueous environments?
What effect does the hydrophobic effect have on protein folding in aqueous environments?
What is the name of the AI network developed by Google AI offshoot DeepMind for protein structure prediction?
What is the name of the AI network developed by Google AI offshoot DeepMind for protein structure prediction?
In protein folding, what disrupts the native structure leading to denaturation due to strong electrostatic repulsion?
In protein folding, what disrupts the native structure leading to denaturation due to strong electrostatic repulsion?
How do membrane proteins typically differ from globular proteins in terms of hydrophobic residues?
How do membrane proteins typically differ from globular proteins in terms of hydrophobic residues?
Which phenomenon describes the tendency of nonpolar molecules to aggregate in an aqueous environment?
Which phenomenon describes the tendency of nonpolar molecules to aggregate in an aqueous environment?
What is a common factor among fibrous proteins?
What is a common factor among fibrous proteins?
What term was first coined by A.Wada and M.Ohgushi in 1983 to describe a phase of proteins that conserves a native-like secondary structure content without the tightly packed protein interior?
What term was first coined by A.Wada and M.Ohgushi in 1983 to describe a phase of proteins that conserves a native-like secondary structure content without the tightly packed protein interior?
What is the main challenge in predicting protein structures?
What is the main challenge in predicting protein structures?
What is the role of molecular chaperones in protein folding?
What is the role of molecular chaperones in protein folding?
Which factor is most likely to contribute to the denaturation of a protein?
Which factor is most likely to contribute to the denaturation of a protein?
Which factor can lead to denaturation of proteins?
Which factor can lead to denaturation of proteins?
What role do molecular chaperones play in the context of protein folding?
What role do molecular chaperones play in the context of protein folding?
How do membrane proteins differ from globular proteins in terms of hydrophobic residues?
How do membrane proteins differ from globular proteins in terms of hydrophobic residues?
Which type of proteins are often rich in hydrophobic residues?
Which type of proteins are often rich in hydrophobic residues?
Which of the following statements best describes the hydrophobic effect in protein folding?
Which of the following statements best describes the hydrophobic effect in protein folding?
What effect does the hydrophobic effect have on protein folding in aqueous environments?
What effect does the hydrophobic effect have on protein folding in aqueous environments?
What is the primary cause of denaturation in proteins?
What is the primary cause of denaturation in proteins?
What is the role of molecular chaperones in protein folding?
What is the role of molecular chaperones in protein folding?
Which factor is NOT involved in protein denaturation?
Which factor is NOT involved in protein denaturation?
How do membrane proteins differ from globular proteins in terms of hydrophobic residues?
How do membrane proteins differ from globular proteins in terms of hydrophobic residues?
What contributes to diseases like Alzheimer's and Type 2 Diabetes?
What contributes to diseases like Alzheimer's and Type 2 Diabetes?
In protein folding, what role do chaperones play?
In protein folding, what role do chaperones play?
What type of interactions are involved in the tertiary structure of proteins?
What type of interactions are involved in the tertiary structure of proteins?
What distinguishes membrane proteins from globular proteins?
What distinguishes membrane proteins from globular proteins?
What can cause denaturation of proteins?
What can cause denaturation of proteins?
What effect does the hydrophobic effect have on proteins in water?
What effect does the hydrophobic effect have on proteins in water?
What structural element causes a bend or kink in an alpha helix?
What structural element causes a bend or kink in an alpha helix?
Which amino acid is primarily responsible for disrupting the alpha helix structure due to the lack of an N-H group for hydrogen bonding?
Which amino acid is primarily responsible for disrupting the alpha helix structure due to the lack of an N-H group for hydrogen bonding?
What is the primary cause of disruption in an alpha helix structure due to strong electrostatic repulsion?
What is the primary cause of disruption in an alpha helix structure due to strong electrostatic repulsion?
Which factor disrupts the alpha helix due to restricted rotation from its cyclic structure?
Which factor disrupts the alpha helix due to restricted rotation from its cyclic structure?
What causes disruption in an alpha helix structure due to steric crowding?
What causes disruption in an alpha helix structure due to steric crowding?
Which type of protein structure is significantly impacted by proline due to its cyclic structure and lack of an N-H group for hydrogen bonding?
Which type of protein structure is significantly impacted by proline due to its cyclic structure and lack of an N-H group for hydrogen bonding?
Which component of an alpha helix structure is disrupted by the absence of N-H groups for hydrogen bonding?
Which component of an alpha helix structure is disrupted by the absence of N-H groups for hydrogen bonding?
In protein structures, what does proline disrupt due to strong electrostatic repulsion?
In protein structures, what does proline disrupt due to strong electrostatic repulsion?
What disrupts an alpha helix structure due to steric crowding caused by bulky side chains proximity?
What disrupts an alpha helix structure due to steric crowding caused by bulky side chains proximity?
Study Notes
Protein Structure
- Primary (1°) structure: the sequence of amino acids in a polypeptide chain, read from the N-terminal end to the C-terminal end.
- Secondary (2°) structure: local conformations, maintained by extensive hydrogen bonding that involves components of the peptide bond.
- 2 types of 2° structures: α-helices and β-sheets.
- α-helices: helical, coiled structures formed by hydrogen bonds between C=O and N-H groups of amino acids.
- β-sheets: extended, flat structures formed by hydrogen bonds between amino acids.
- Tertiary (3°) structure: the completely folded and compacted polypeptide chain, stabilized by interactions of amino acid side chains.
- Forces involved: hydrogen bonding, electrostatic interactions, hydrophobic interactions, and disulfide bonds.
- Quaternary (4°) structure: the association of polypeptide chains (sub-units) combining together.
- Example: hemoglobin has 4 sub-units (α and β) that bind 4 O2 molecules.
Protein Folding
- Chaperones: part of a quality control system that ensures proper protein folding or restores misfolded proteins after stress.
- Denaturation: the loss of structural order that gives a protein its biological activity.
- Caused by: pH changes, Mercaptoethanol, detergents, heat, and urea/guanidine.
- Renaturation: the process of returning to the native structure after denaturation.
Protein Folding and Disease
- Protein aggregation: linked to numerous neurodegenerative diseases.
- Molten globule: a third phase of proteins, characterized by a native-like secondary structure content but without a tightly packed protein interior.
Prediction of Protein Structure
- Structure prediction challenge: a biennial challenge to predict protein structures from amino acid sequences.
- AlphaFold: an AI network developed by Google AI that outperformed other teams in the CASP challenge.
Protein Functions
- Globular proteins: water-soluble, spherical proteins with polar side chains on the outside and non-polar side chains inside.
- Fibrous proteins: insoluble, strong, and structurally important proteins, such as keratin and collagen.
Hemoglobin and Myoglobin
- Hemoglobin: a protein in blood with 4 sub-units, binds 4 O2 molecules, and exhibits cooperativity and pH-dependent O2 binding.
- Myoglobin: a protein in muscle and tissue, binds 1 O2 molecule, and has no quaternary structure.
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Description
Explore the components of protein structure including primary, secondary, tertiary, and quaternary structures. Learn about a-helices, b-sheets, protein folding, and the levels of protein structure.
