Proteins Flashcards
Proteins
20 amino acids
non polar
hydrophobic and with two hydrocarbon side chains
polar
hydrophilic with ionic side chains
peptide bond
links two ore more amino acids together
amino acid
n-c-c
Primary Structure
sequence of amino acids
Secondary Structure
Alpha Helix, Beta Plate Sheet
Tertiary Structure
Globular proteins
Quanternary Structure
two globular proteins held together
Denaturation
the disruption of bonds in secondary, tertiary and quantary structures
Enyzmes
Biological Catalysts
oxidreduces
oxidation/reduction
Transferases
transfer of atoms
Lyases
ass/remove from a double bond
Hydrolases
Hydrolysis
Isomerases
rearrange atoms
Ligases
use ATP to combine small molecules
active site
where the substrate catalyzes the reaction
lock and key model
active site is rigid, non flexible shape only for the substrate to fit in
Induced fit model
enzy,e changes shape to fit the substrate more tightly
optimum Ph for enzymes
7.4
optimum temp for enzymes
37 C
Competitive inhibitors
inhibitor fights the substrate and forms in the active site
non competitive inhibitor
goes to the other side of a enzyme to change its shape of the active site
