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50 Cards in this Set
- Front
- Back
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What are the two biochemical forces? |
Covalent and Noncovalent bonds |
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Covalent bonds |
strong, 200-800 kj/mol |
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Noncovalent bonds |
Ionic, Hydrogen, Hydrophobic, VDW |
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How are acids and bases measured? |
Comparing [H+] and [OH-] |
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Equation to find pH |
pH=-log[H+] |
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How do you know if something is basic? |
[OH-]>[H+] |
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How do you know if something is acidic? |
[H+]>[OH-] |
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When pH=pKa... |
[HA]=[A-] |
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What is dialysis? |
-Used to separate proteins from small solutes -Takes advantage of passive diffusion through a semi-permeable membrane |
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What is column chromotography? |
Method of separating proteins from one another |
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The speed in which a protein passes through the column depends on what? |
How the protein interacts with both the mobile and stationary phase |
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In ion exchange chromatography what is in the stationary phase? |
Cation exchangers and anion exchangers |
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In size exclusion chromatography what is in the stationary phase? |
Porous polymer beads |
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In size exclusion chromatography, will small or large proteins elute faster? |
Large |
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In affinity chromatography what is in the stationary phase? |
Polymer bound ligand |
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What is SDS Page? |
Separation of proteins by their molecular weight |
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What is SDS? |
Sodium Dodecyl Sulfate Binds to proteins in amounts proportional to the proteins molecular weight Contributes a large net negative charge->the original charge of the protein no longer matters Now each protein has similar charge to mass ratio |
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What is the gel made of in SDS page? |
Cross linked polymer polyacryl amide |
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What are the 5 steps in sequencing proteins |
1. Beak and block disulfide bonds 2. Cleave proteins into smaller peptides 3. Separate smaller peptides from one another 4. Sequence the smaller peptides 5. Align the peptide sequence |
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1. Break and Block Disulfide Bonds |
Two steps: 1. The reduction step breaks the disulfide bond 2. The alkylation step: Iodoacetic acid binds to the thiol groups on the cysteine residues of the protein, prevents the reformation of the disulfide bonds |
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2. Cleave the proteins into smaller peptides |
Proteases catalyzes the hydrolytic cleavage of peptide bonds
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Are cleavage sites are specific to particular amino acid residues? |
Yes |
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What is the stationary phase of reversed phase chromatography? |
Hydrophobic |
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What is the mobile phase of reversed phase chromatography? |
Hydrophilic |
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What is Edman Degradation |
Amino acid residues are removed from the N-terminus one at a time Identify each residue as it is removed using chromatography Repeat cycle until the sequence is obtained |
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What is 2-D electrophoresis? |
Effective in isolating a particular protein out of a solution of many proteins |
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In 2-D electrophoresis what are the dimensions that the proteins are separated by? |
pI and mass |
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What is the Bohr effect? |
As the concentration of H+ rises, certain amino acid residues on hemoglobin are protonated
Promotes the release of oxygen by favoring a transition to the T state |
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What are enzymes and what do they do? |
Biological catalyst that increase the rate of reaction by lowering the activation energy |
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True or false: Most enzymatic reactions are not bimolecular |
False |
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What is Km? |
Binding affinity constant |
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What is Vmax? |
Maximum rate of a reaction with increasing substrate
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What is Kcat? |
how fast an enzyme creates a product per unit time |
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What are the two types of allosteric control? |
Homotropic and Heterotropic |
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What is homotropic? |
Regulator is substrate the enzyme acts upon |
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What is heterotropic? |
Regulator that is something else other than S |
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What is covalent modification? |
Group addition |
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Glucose |
Important for energy. and building other macromolecules
Precursors for biomolecules and energy |
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Lipids |
Do not polymerize
Group together to form larger structures
Fatty acids and glycerol
Hydrocarbon tails that are hydrophobic and hydrophilic head
Roles are energy storage, synthesis or hormones, vitamins, membranes and used in signaling |
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What is potential energy? |
Energy in between chemical bonds |
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What is enthalpy? |
H, reflects the number and kind of bonds that possess energy |
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What is the first law of thermodynamics? |
Energy cannot be created or destroyed, only transformed or transferred |
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What is the second law of thermodynamics? |
All physical and chemical processes go from a state of order to disorder |
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What is entropy? |
S, randomness of disorder
Natural process tend to raise S |
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What is free energy? |
G, around of energy available to do work |
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What is endergonic? |
Input energy to drive reaction |
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What is exergonic? |
Release of energy |
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Equation to calculate Kc? |
Kc=([C]^c[D]^d)/([A]^a[B]^b) |
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Equation to calculate Ke |
Ke=e^(-DeltaG/RT) |
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Describe the structure of ATP (4) |
1. Electrotstatically repulsive
2. Multiple resonance structures
3. Proton Release
4. Hydration Stabilization |
