Unit 3: Proteins and Enzymes Flashcards
Enzymatic Proteins
Catalyzes (speeds up) reactions
Defensive Proteins
Antibodies that destroy viruses
Storage Proteins
Store Amino Acids (ex: casein in milk)
Transport Proteins
Proteins that transport O2 and other molecules
Amino Acid Formulas
R group, Amino group, and Carboxyl group
Amino acid polymer
polypeptides
peptide bond
the covalent bond that attached polypeptides together
Primary Structure
sequence of amino acids
Primary Structure
sequence of amino acids
Secondary structure
stabilization using hydrogen bonds
α helix and β pleated sheet
Tertiary Structure
3D shapes stabilized by side chain interactions
Quaternary Structure
interactions between polypeptides
Diffusion
greater to lesser concentration
no membrane involved
Osmosis
Moving water molecules from greater to lesser concentration through semi-permeable membranes
Semi-permeable membrane
small, non-polar molecules can go through
Passive transport
transport that does not require energy.
uses concentration gradient
Active transport
requires ATP. goes against concentration gradient.
Chemical Equilibrium
equal concentration of molecules throughout the cell and outside the cell.
Facilitative diffusion
passive transport aided by channel and carrier proteins
Carrier proteins
shape change that translocates the solute binding site across the membrane
ATP
energy form: adenosine tri-phosphate
Membrane potential
the voltage across a membrane
Proton pump
actively transports H+ OUT of the cell
Cotatransport
couples the downhill diffusion of solute to uphill transport against concentration gradient
Active Site
The location where a substrate and an enzyme react
Substrate
the molecule upon which the enzyme acts (ex: H2O2 Hydrogen Peroxide)
Pepsin
Enzyme in stomach that breaks down peptide bonds
Lock and Key Model
Enzyme and Substrate
Induced Fit (Hand and Glove)
Substrate and Enzyme
Competitive Inhibitor
Fits into and blocks active site
Non-competitive inhibitor
Folds protein over active site by attaching to side of protein
