20 Questions
What stabilizes the folded structure of a protein?
Noncovalent interactions
What is the term for the compact three-dimensional regions in the structure of a protein?
Protein domains
What do we call a protein that catalyzes the formation or breakage of a specific covalent bond in a ligand?
Enzyme
What induces a significant change in protein shape outside of the active site of an enzyme?
Binding of small ligands
What is the term for the regulation of an enzyme by the binding of one of the pathway's end products?
Feedback inhibition
Which type of proteins act as molecular switches that are active with GTP bound and inactive with GDP bound?
GTP-binding proteins
What type of proteins can exist in two conformations that differ in catalytic activity and can be turned on or off by ligands?
Allosteric proteins
Which process controls the location and function of a protein and can serve as docking sites for other proteins?
Covalent modifications
What type of protein machines are formed by assemblies of allosteric proteins to perform complex functions?
Allosteric protein machines
What forms as phase-separated biomolecular condensates, speeding important reactions and confining them to specific regions of the cell?
Biochemical subcompartments
What is the term for the unique amino acid sequence of a protein that determines its three-dimensional shape and biological activity?
Protein primary structure
Which type of interaction stabilizes the folded structure of a protein through hydrogen bonds between neighboring regions of the polypeptide backbone?
Hydrophobic interactions
What do we call the small ligands that can induce a significant change in protein shape outside of the active site of an enzyme?
Activators
What term is used for the compact three-dimensional regions within the structure of a protein, which are known to exist as independent folding units?
Tertiary domains
What type of regulation involves an enzyme being inhibited by the binding of one of the pathway's end products?
Allosteric regulation
Which proteins act as molecular switches, being active when GTP is bound and inactive when GDP is bound?
GTP-binding proteins
What type of proteins form highly efficient protein machines through coordinated conformational changes?
Allosteric proteins
What controls the location and function of a protein and can serve as docking sites for other proteins?
Covalent modifications
What produces directed movement in eukaryotic cells through conformational changes linked to the hydrolysis of a tightly bound molecule of ATP to ADP?
Motor proteins
What form as phase-separated biomolecular condensates, speeding important reactions and confining them to specific regions of the cell?
Biochemical subcompartments
Test your knowledge about the structure of proteins, the diversity of amino acid sequences, and the noncovalent interactions that stabilize the folded structure of proteins.
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