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Questions and Answers
Which type of noncovalent interaction can be found between backbone elements of the polypeptide or between amino acid side chains? Select one:
Which type of noncovalent interaction can be found between backbone elements of the polypeptide or between amino acid side chains? Select one:
- Electrostatic interactions
- Van der Waals attractions
- Hydrophobic forces
- Hydrogen bonds (correct)
Which free energy value (G) would correspond to the folded protein structure with the most stable conformation? Select one:
Which free energy value (G) would correspond to the folded protein structure with the most stable conformation? Select one:
- 5
- 10
- 1 (correct)
- 15
If protein folding is determined by the sequence of amino acids in the polypeptide chain, why are chaperone proteins needed to assist folding in the cell? Select one:
If protein folding is determined by the sequence of amino acids in the polypeptide chain, why are chaperone proteins needed to assist folding in the cell? Select one:
- Protein folding is energetically unfavorable.
- Proteins constantly unfold and refold.
- Certain proteins easily aggregate with other proteins. (correct)
- Some proteins cannot fold on their own.
Hydrogen bonding between N-H and C=O groups of every fourth amino acid within a polypeptide chain results in which type of folding pattern? Select one:
Hydrogen bonding between N-H and C=O groups of every fourth amino acid within a polypeptide chain results in which type of folding pattern? Select one:
Which of the following is true about amyloid protein structures? Select one:
Which of the following is true about amyloid protein structures? Select one:
A stretch of amino acids in a polypeptide chain that is capable of independently folding into a defined structure is called a? Select one:
A stretch of amino acids in a polypeptide chain that is capable of independently folding into a defined structure is called a? Select one:
Which of the following levels of protein structure involves the interaction of more than one polypeptide chain into a three-dimensional structure? Select one:
Which of the following levels of protein structure involves the interaction of more than one polypeptide chain into a three-dimensional structure? Select one:
Which of the following shows protein organizational units in the correct order from smallest to largest? Select one:
Which of the following shows protein organizational units in the correct order from smallest to largest? Select one:
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Study Notes
Noncovalent Interactions in Polypeptides
- Hydrogen bonds form between polar groups in the polypeptide backbone and amino acid side chains.
- Hydrophobic forces and electrostatic interactions do not typically involve the polypeptide backbone due to its uncharged polar nature.
Free Energy in Protein Folding
- The most stable protein conformation corresponds to the lowest free energy value, G=1.
- A decrease in free energy during protein folding indicates an energetically favorable process.
Role of Chaperone Proteins
- Certain proteins require assistance from chaperone proteins to fold correctly in crowded cellular environments.
- Chaperones help prevent aggregation of proteins that could hinder proper folding due to favorable interactions before folding occurs.
Protein Folding Patterns
- The alpha helix structure forms through hydrogen bonding between every fourth amino acid in the polypeptide chain.
- Beta-pleated sheets result from hydrogen bonding between segments of the polypeptide chain but involve different amino acids.
Amyloid Protein Structures
- Amyloid structures are characterized by interlocking stacked beta sheets.
- While some amyloid proteins are associated with diseases, not all amyloid structures cause neurodegenerative conditions.
Definition of a Domain
- A domain in a polypeptide chain can independently fold into a defined structure due to side-chain interactions.
- Domains differ from subunits; a subunit refers to complete polypeptide chains that form larger complexes.
Levels of Protein Structure
- Quaternary structure involves the assembly of multiple polypeptide chains into a three-dimensional complex.
- Primary structure refers to the amino acid sequence, while secondary and tertiary structures describe organized arrangements and overall shape, respectively.
Organizational Units of Proteins
- The correct order of protein organizational units from smallest to largest is: domain < subunit < complex.
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