Exam 1 Flashcards
Polar molecules are…
hydrophilic
The four weak bonds are:
Ionic, Hydrogen, Hydrophobic, Van der Waals
What is PAGE-SDS?
Electrophoresis: Used to isolate fragments that contain a gene of interest
What is electronegativity?
The attraction of electrons to a certain molecule
What is a peptide bond?
A covalent bond between an amino group (N terminus) of one AA and a carboxyl group (C terminus) of another AA
How do peptide bonds occur?
Dehydration synthesis (removal of water)
What is the primary structure?
Sequence of amino acids to form polypeptide chain
What is the secondary structure?
An alpha helix OR beta sheet (ONLY BACKBONE (NO R GROUP))
What is the tertiary structure?
More compact, R groups interacting, all weak bonds AND disulfide bonds. Folding of domains based on hydrophilic/phobic interactions.
What is the quaternary structure?
Polypeptides all bonded, in one group
What is a domain?
any segment of a polypeptide chain that can fold into a compact, stable structure
What purposes do proteins serve?
Enzymes, structural, transport, storage etc…
What is the effect of temperature on proteins?
More heat -> increased kinetic energy (proteins move around more), too much = protein denatures
What is the effect of pH on proteins?
Change of concentration, changes how the amino acids bind to one another, changes charge of protein/function
What is ligand binding?
Binds two receptor proteins and can change the shape/conformation of the protein.
What is the difference of anabolism vs catabolism?
Catabolism breaks down large molecules and RELEASES energy, while anabolism builds large molecules and REQUIRES energy
What is metabolism?
All chemical reactions that occur in a cell to transform matter and energy
What is the formula for change in G?
ΔG = ΔH - TΔS
What is Gibbs Free Energy?
The energy available to produce useful work
What is ΔH?
It is enthalpy, or the energy contained in chemical bonds
What is ΔS
It is enthropy, or the amount of disorder (heat released)
If ΔG is less than 0…
The reaction will occur spontaneously (energetically favorable)
If ΔG is more than 0…
The reaction will not occur spontaneously (not energetically favorable)
How do enzymes work?
Enzymes attract substrates to the active site, then catalyzes the chemical reaction, and breaks down the substrate so it can form new bonds!!!
What is an induced fit model?
Also known as the “Enzyme Substrate Complex”, a combined structure of the enzyme and its substrate bound to the active site
What are cofactors?
Small and inorganic molecules which help enzyme function
What are coenzymes?
Organic molecules that bind to the active site to help finalize the shape of the site
What are inhibitors?
Molecules that reduce the activity of an enzyme (they INHIBIT the enzyme)
What are the two types of inhibitors?
Competitive inhibitor (interferes directly with the active site)
Allosteric inhibitor (interferes indirectly to active site, changes shape of enzyme at allosteric site (other part))
What are coupled reactions?
Energy transferred from one reaction to another (EXAMPLE ATP COUPLING)
What are sugars?
They are a quick energy source
Name some important disaccharides.
Sucrose, Maltose, Lactose
Name some important polysaccharides.
Starch, Glycogen, Cellulose, Chitin, Peptidoglycen
What are the roles of lipids?
Long term energy storage (triglycerols), structural (phospholipids), hormones (steroids)
What are the four family groups of lipids?
Triglycerides, phospholipids, steroids, and waxes
What is a triglyceride?
Formed from one glycerol molecule, bond to 3 fatty acid molecules (lots of bonds, better for energy storage)