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31 Cards in this Set
- Front
- Back
Type of amino acids found in nature?
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L-amino acids
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Highly Hydrophobic AAs
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IsoValLeuPheMet
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Less Hydrophobic
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AlaGlyCysTrpTyrProThrSer
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Highly Hydrophilic
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HisGluAsnGlnAspLysArg
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Paralogs
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Present within one species, different functions
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orthologs
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present within diff species, same function
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primary structure forces
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peptide bonds
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secondary structure forces
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H-bonds, van der waals
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tertiary structure forces
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covalent bonds (disulfide bridges), non-cov interactions(electrostatic, van der waals, hydrophobic)
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quaternary structure forces
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covalent bridges, non covalent interactions
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proteins can be denatured by
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heat, extreme changes in pH, chemicals (SDS, urea, mercaptoethanol)
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ion exchange
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polymer beads with charged groups
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gel filtration
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porous beads, smaller get stuck, larger pass through
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affinity
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polymer bound ligand for protein of interest
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Electrophoresis - reagent? which move further, larger or smaller
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SDS added. Larger move slower, since they are held up by the gel
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SDS Page Axises
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X right, decreasing pH
Y down, decreasing Mw |
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How can Cystine bridges be broken?
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oxidation by performic acid
or reduction by DTT, then acetylation by iodoacetate |
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What reagents determine the N-terminal amino acid only?
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flurodinitrobenzene, dabsyl chloride, dansyl chloride
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What reagent is used for edman degradation?
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phenyl isothiocyanate
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Where does trypsin break?
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C-Lys, Arg
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Where does chymotrypsin break?
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C-Phe,Trp,Tyr
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Where does staph protease break?
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C-Asp,Glu
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Where does cyanogen bromide break?
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C-Met
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enzyme units
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the amount of enzyme, that, under defined conditions, will catalyze the trans of 1 umol of substrate per min
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specific activity
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number of enzyme units per mg
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Michaelis-menton equation
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V0=Vmax*[S] / Km+[S]
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Michaelis constant
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Km=(k2)+(k-1)/(k1)
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Lineweaver-burk equation
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1/V0=Km/Vmax * 1/[S] + 1/Vmax
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Effect of 2,3BPG on hemoglobin
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binds in a cleft in T form, stabilizing it, reducing O2 affinity
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Effect of H+ on hemoglobin
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favors T state, releasing O2
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Carbonic anhydrase equation
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H+ + HCO3- <--> CO2 + H20
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