Hierarchical Structure, Folding, Modification, & Degradation of Proteins Flashcards
genome
entire DNA/RNA of an organism; same in every cell type
proteome
protein compliment within an organism or individual cell types
polypeptide
chain of amino acids
Protein folding is dependent on…
the linear arrangement of amino acids.
primary structure
sequence of amino acids
secondary structure
polypeptide folded based on aa sequence
tertiary structure
arrangement of secondary structures into domains
quaternary structure
formed when two or more proteins interact
amino acid components
central carbon amine group carbonyl group hydrogen R group
N-terminus
amino end
C-terminus
carboxyl end
Tertiary structure is held together by…
hydrophobic interactions, hydrogen bonds, and peptide bonds.
motif
small region of conserved sequence that will fold for a certain function
domain
large distinct section of a protein that differs in structure and function
amphipathic
one side of protein is hydrophilic & other is hydrophobic; allows coils to wrap around each other
protein families
share conserved structure and therefore common function
native state
most stable folded confirmation of a protein
denaturation
disruption of interactions holding conformation
chaperone
binds/stabilizes unfolded protein to prevent degradation & encourage proper folding
chaperonin
macromolecular machine that binds a protein and facilitates proper folding
acetylation
modification or free amino terminus; alters half-life
lysosomal degradation pathways
endocytosis, phagocytosis, autophagy
endocytosis
uptakes small molecules
phagocytosis
uptake of bacteria
autophagy
degradation of cell components for recycling (has double lipid bilayer)
proteasome-directed degradation
macromolecular machine that degrades poly-ubiquitinated proteins
ubiquitin
76 amino acid polypeptide; covalently attaches to lysine residues