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14 Cards in this Set
- Front
- Back
Define specific activity
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ratio of activity to total mg of protein (measured in biological/chemical processes)
increases as purity increases assay = determine specific activity |
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How re cells fractionalized?
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1) grind
2) freeze/thaw 3) high freq. sound waves 4) high pressure 5) hydrolysis of cell wall, lyse membrane (bacteria) 6) if secretes centrifuge to separate |
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common purification methods
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1) bulk methods (salt out)
2) molecular sieve 3) ion exchange chromatography (charge of molecule) 4) disc electrophoresis - size and charge 5) affinity chromatography |
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affinity chromatography
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interactions between molecule of interest and compound
ex: bind molecule of interest to enzyme and filer out *use later on with more pure compound to prevent interactions |
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describe denaturation
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*does not affect primary structure
1) heat - destroys alpha and beta sheets 2) chemicals - break H bonds (2) 3) Reducing agents - break disulfide bonds (3) 4) heavy metal ions - attack salt bridges (3) alcohol - coagulates |
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primary structure
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sequence of aa = polypeptide chain
each protein is unique responsible for other structures starts at n-terminus, finishes at c-terminus |
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secondary structure
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H bonding between alpha (springs) and beta (sheets)
bonds between peptide backbone repeating patterns |
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tertiary structure
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interactions of side chains
bonds: covalent, H,salt bridges, hydrophobic interactions, metal ion coordination 3d |
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quaternary structure
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polypeptide subunits form a whole
only proteins with subunits ex: hemoglobin, collagen, integral membrane proteins |
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covalent bonds
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disulfide bonds
link between two chains or two parts of the same chain (share electrons) |
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hydrogen bonding
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between backbone -C=O and -N-H groups
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salt bridges
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2 amino acids with ionized side chains
or acidic + basic aa |
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hydrophobic interactions
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polar groups outward, nonpolar inwards
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metal ion coordination
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2 side chains with same charge linked
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