26 Questions
What characteristic prevents free rotation around the bond between the carbonyl carbon and the nitrogen of the peptide bond?
Rigidity and planarity
Which condition is required to non-enzymatically hydrolyze peptide bonds?
Prolonged exposure to a strong acid or base at elevated temperatures
What term is used to describe each component amino acid in a polypeptide?
Residue
What stabilizes an α-helix structure by extensive hydrogen bonding between the peptide-bond carbonyl oxygens and amide hydrogens?
Hydrogen bonds
What type of secondary structure forms when two or more separate polypeptide chains are arranged in parallel or antiparallel to each other?
β-Sheet
What is the name of the linear sequence of linked amino acids in a protein?
Primary structure
Why is understanding the primary structure of proteins important?
To identify genetic diseases associated with abnormal amino acid sequences
What type of bond joins amino acids together in proteins?
Peptide bond
What results from the linkage of many amino acids through peptide bonds?
Polypeptide
What type of bond joins amino acids together in proteins?
Peptide bond
What is the name of the level of protein structure that involves the sequence of amino acids in a protein?
Primary
What is the convention for naming the ends of a peptide chain?
Free amino end to the left, free carboxyl end to the right
What condition results in proteins with abnormal amino acid sequences, causing improper folding and loss of normal function?
Abnormal primary structure
What characteristic prevents free rotation around the bond between the carbonyl carbon and the nitrogen of the peptide bond?
Rigid structure
What is the convention for writing the free amino end (N-terminal) and the free carboxyl end (C-terminal) of a peptide chain?
(N-terminal) on the left and (C-terminal) on the right
Which type of structure forms when two or more separate polypeptide chains are arranged in parallel or antiparallel to each other?
Beta-sheet
What term is used to describe the portion of the amino acid remaining after the atoms of water are lost in the formation of the peptide bond?
Residue
What is required to non-enzymatically hydrolyze peptide bonds?
Prolonged exposure to a strong acid or base at elevated temperatures
What type of bond has a partial double-bond character and is shorter than a single bond?
Peptide bond
Which structure is stabilized by extensive hydrogen bonding between the peptide-bond carbonyl oxygens and amide hydrogens?
α-Helix
What is the term for the spiral structure consisting of a tightly packed, coiled polypeptide backbone core, with the side chains of the component amino acids extending outward?
α-Helix
How many amino acids are contained in each turn of an α-helix?
3.6
What type of secondary structure is formed by two or more separate polypeptide chains that are arranged in parallel or antiparallel to each other?
β-Sheet
What type of sheet appears 'pleated' due to the almost fully extended segments of polypeptide chains involved in hydrogen bonding?
Antiparallel sheet
What characteristic prevents free rotation around the bond between the α-carbons in the polypeptide chain?
Rigid and planar structure
What type of bond helps reverse the direction of a polypeptide chain, aiding in the formation of a compact, globular structure?
Hydrogen bond
Test your knowledge about protein structures with a focus on the primary, secondary, tertiary, and quaternary levels of organization. Understand how amino acids are joined together by peptide bonds to form unique three-dimensional shapes.
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