Proteins Flashcards

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1
Q

What is a dipeptide?

A
  • 2 amino acids join
  • NH2 group bonds with COOH group
  • Condensation reaction
  • Peptide bond
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2
Q

Primary Structure of Protein?

A

Order of amino acids, it is specific

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3
Q

All I need to know about secondary structure of Proteins.

A
  • Hydrogen bonding between Nδ- and Oδ- react with Hδ+
  • Forms α-helix or β-pleated sheet
  • α-helix shape when H bonds form between every 4th peptide bond
  • β-pleated sheet shape forms when protein folds so 2 polypeptide chains are parallel
  • Collagen and keratin have secondary structure
  • H bonds can be broken by high temps and pH changes
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4
Q

All I need to know about tertiary structures of Proteins.

A
  • Hydrogen bonds (only R groups)
  • Disulphide bonds (cysteine amino acids)
  • Ionic bonds (charged R groups)
  • Weak hydrophobic interactions (polar R groups)
  • Common in globular proteins
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5
Q

How do we hydrolyse proteins?

A
  • Condensation Reaction
  • H2O added to molecule
    Concentrated HCL used
  • Mixture boiled for many hours
  • With enzymes, at room temp
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6
Q

All I need to know about Thin Layer Chromatography

A
  • Amino acids identified by their varying R groups
  • TLC plate sprayed with locating agent (staining amino acids) or illuminated by UV light
  • Rf value calculated
  • Compared to analytical data to deduce composition of mixtures
  • If Rf values too similar for 2 amino acids, 2D TLC can be used
  • Run through first solvent, turned 90 degrees and run through 2nd.
  • 2 Rf values gives greater confidence determining amino acid
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