BCHM 307

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Author:
Anonymous
ID:
235197
Filename:
BCHM 307
Updated:
2013-09-16 19:40:38
Tags:
Slide thirty eight
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Description:
protien denatureing
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  1. Denaturing agent Target:
    heat
    agitation
    pH
    mercaptoethanol
    detergents
    SDS
    Urea guanidine HCl
    • H-bonds, Hydrophobic interactions
    • H-bonds, Hydrophobic interactions
    • salt bridges
    • disulfide bridges
    • hydrophobic interactions
    • H-bonds, Hydrophobic interactions
  2. Quaternary Structure
    • dimers, trimers, tetramers
    • homodimer/heterodimers
    • heterotetramer
  3. Cooperativity
    • Like hemoglobin
    • either all on or all off
    • the more it gets the easier it is to get more
  4. daltons
    the size or molecular weight of protein as a sum of its AA
  5. Gel Filtration Chromatography
    • Doesn't denature the protein
    • separates based on affinity to phases
    • the smaller the particle the longer it takes
    • increases volume- spreads out
  6. Ion Exchange Chromatography
    • beads have charge
    • can have very low concientration
    • can elute bound compounds with gradient of counter ions (∆pH or increase NaCl content)
  7. UV Absorbance Monitored
    • during chromatography
    • each aa absorbs light at different wavelengths
  8. Enzymes are Catalysts 3 general
    • Increase rate of rxn (1020 fold)
    • not consumed by the rxn
    • act repeatedly to increase rate
  9. Enzymes work by...
    • Not ∆ equ constant
    • Not ∆ amount of energy consumed/liberated in rxn
    • Do increase rate rxn that can already happen
    • Do decrease activation energy

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