Protein Structure - 5.4 Flashcards
Functions of Proteins
Defense, enzymes, structure, movement, signaling, transport, regulation
monomers of protein
amino acid
polymer of protein
peptides, polypeptides, proteins
structure composed of
alpha carbon, carboxyl (cooh) group, amino (nh2) group, R group
Some r groups are hydrophobic…so they’re
nonpolar
Some r groups are hydrophilic…so they’re
polar
Neg charged side chain means
side chain is acidic
coo
hydrophillic
Pos charged side chain means
side chain is basic
amino
hydrophillic
polymerization of amino acids is
the formation of a peptide bond (covalent bond)
Polymerization occurs on
ribosomes
Primary structure
sequence of amino acids
secondary structure
coils + folds in the polypeptide chain (bc H bonds between backbone atoms)
Flexible A helices and rigid B sheets
tertiary structure
-interactions among various side chains (R groups)
folds into specific 3D, compacted shape
-interactions among R groups of amino acids stabilizes tertiary structure
quaternary structure
when a protein consists of multiple polypeptide chains
hemoglobin
disulfide bridges occur between ___ do what?
cysteines
stabilizes the protein structure
interactions between polypeptides are
NONcovalent
protein structure influenced by
temperature, pH, salt concentration
what makes the protein inactive
destroying weak bonds/interactions that maintain 3D structure
bond between amino acids
peptide bond
tertiary structure - ionic bonds form between
basic and acidic amino acids
ex: lysine and glutamic acid
lysozyme
enzyme that helps prevent infection by biding to and destroying specific molcules on the surface of bacteria
Folding of the chain influenced by
formation of various bonds between parts of the chain
amino acids with non polar (hydrophobic) side chains end up
at the core of the protein (away from water)
called hydrophobic interactions
Cluster of hydrophobic side chains held together by
van der waals interactions
____ between polar side chains
Hydrogen bonds
_____ between + and - charged side chains
ionic bonds
denaturation
protein unravels and loses its native shape
inactive