Use LEFT and RIGHT arrow keys to navigate between flashcards;
Use UP and DOWN arrow keys to flip the card;
H to show hint;
A reads text to speech;
47 Cards in this Set
- Front
- Back
|
Gibbs Free Energy Equation |
G = H-TS |
|
|
Gibbs Free Energy Trends |
H (-) and S (+) Always Spontaneous H (+) and S (-) Never Spontaneous H (+) and S (+) Spontaneous at high temperatures H (-) and S (-) Spontaneous at low temperatures |
|
|
Only thing that affects the thermodynamics of a reaction |
Temperature |
|
|
(+) Gibbs Free Energy |
Endergonic and non spontaneous |
|
|
(-) Gibbs Free Energy |
Exergonic and spontaneous |
|
|
(+) Enthalpy |
Endothermic Break Bonds |
|
|
(-) Enthalpy |
Exothermic Make Bonds |
|
|
(+) Entropy |
Increase in Disorder Spontaneous More products than reactants Change to higher entropy State (g>l>s) |
|
|
(-) Entropy |
Decrease in Disorder Non Spontaneous |
|
|
Energy of Activation |
energy to achieve the transition state affects the kinetics larger Ea, slower reaction decrease by adding catalysts which lowers the transition state and does nothing to the thermodynamics of the reaction |
|
|
Enzyme |
Stabilizes transition state by Amino Acid on the active site Made of Proteins or RNA (Ribosome) |
|
|
Active Site |
Where the substrate binds and reaction is catalyzed |
|
|
Allosteric Site |
other than the active site. Inhibition or activation (basically regulation) |
|
|
Enzyme Activity Affected by: |
Temperature: increases activity until denaturation pH: All enzymes have optimal pH Co-factor (inorganic) and Co-enzyme (organic) Substrate concentration |
|
|
Regulation of Enzyme |
Covalent Modification: Adding (Kinase) or Removing (phosphatase) Pi (inorganic phosphate) Association with other polypeptides Proteolytic Cleavage (ase): Think zymogens which are inactive enzymes that end in ogen or begin with pro. They need to be activated Allosteric: bind to the site |
|
|
Inhibition of Enzyme: velocity graph: At the plateau |
Substrate saturated enzyme (only so many given enzymes present)
This the Vmax |
|
|
Vmax affected by |
the number of enzymes |
|
|
Km |
substrate affinity for the enzyme number of enzymes does not affect it lower Km, higher the affinity if moves right, lower affinity because taking longer to get to Vmax |
|
|
Types of Inhibition: Competitive |
Inhibitor competes with the substrate for the active site Enzyme is unaffected so no change to Vmax Substrate doesn't bind as easily so affinity decreases and Km increases |
|
|
Types of Inhibition: Noncompetitive |
inhibitor binds to the allosteric site and deactivates enzyme the enzyme number is lowered so Vmax decreases no change to Km |
|
|
Types of Inhibition: Uncompetitive |
Inhibitor binds to the Enzyme-Substrate Complex More affinity/pressure for substrate to bind so affinity increases and Km decreases Once the inhibitor binds, enzyme deactivated so Vmax decreases |
|
|
Types of Inhibition: Mixed |
Inhibitor binds to enzyme substrate complex or the enzyme depending on what it likes more Vmax: decreases if Enzyme preferred: Km increases (looks like noncompetitive) If E-S preferred: Km decreases (looks like uncompetitive) if equal: Km no change mixed type |
|
|
If AA above isoelectric point |
+1 charge |
|
|
If AA below isoelectric Point |
-1 charge |
|
|
If AA at isoelectric Point |
Zwitterion (no net charge) |
|
|
Acidic Amino Acids |
Have 2 COOH groups so donate extra H Glutamate Asparate |
|
|
Basic Amino Acids |
Have extra amine so can accept extra H Histidine, Argenine, Lysine |
|
|
Polar Amino Acids |
Serine Threonine Asperigine Glutamine |
|
|
Non Polar Amino Acids |
Glycine (only achiral AA) Alanine Valine Leucine Isoleucine |
|
|
Aromatic Amino Acids |
Have a ring Tyrosine (contains phenol) so polar Nonpolar: phenylalanine and Tryptophan |
|
|
Sulfur Containing Amino Acids |
Cysteine Methionine (start codon AUG) |
|
|
Proline |
Most hindered. R group comes back and forms a ring not found in alpha helix because it forms too tight of a turn |
|
|
Peptide Bond |
Amine at the front COOH at the back partial double bond causes resonance and prevents free rotation |
|
|
Hydrolysis to break a peptide bond. Increase rate by |
Enzymes (proteases that are zymogens) Temperature pH (low) |
|
|
Primary Protein Structure |
sequence of amino acids held by peptide bonds |
|
|
Secondary Protein Structure |
B pleated sheets and Alpha helices (protein motifs( Held by hydrogen bonds |
|
|
Tertiary Structure |
3D shape disulfide bridges |
|
|
Quaternary Protein Structure |
Association with other polypeptides. Same bonds as tertiary |
|
|
Proteins |
Only ones to contain sulfur building blocks are amino acids Can only digest L configuration |
|
|
Carbohydrates |
CnH2nOn Aldo and Keto storing energy as sugar and also as water number of stereoisomers: 2^n |
|
|
Determining Chirality |
Last stereocenter (furthest from functional group) Can only digest D (D for delicious) so OH on the right |
|
|
Lipids |
Most energy because tons of electrons head is hydrophilic and tail is hydrophobic |
|
|
Lipids in water |
forms a micelle heads on the outside and tails inside clump into sphere maximize the volume by minimizing the surface area body has to emulsify the fats: bile made by liver and stored and released by gall bladder to emulsify the fats |
|
|
Functions of Lipids |
Energy Storage (more energy stored bc without water closer together) Insulation Cell Membrane: like dissolves like Cholesterol to make steroid hormones |
|
|
Cholesterol |
Precursor for bile and steroid hormones increase the fluidity of the plasma membrane |
|
|
dietary fat broken down into |
2 fatty acids and 1 monoglyceride before absorption |
|
|
DNA Methylation |
Occurs via addition of methyl group to cytosine --> methyl-cytosine-base pairing with guanine |
