Proteins Flashcards
1
Q
What is a dipeptide?
A
- 2 amino acids join
- NH2 group bonds with COOH group
- Condensation reaction
- Peptide bond
2
Q
Primary Structure of Protein?
A
Order of amino acids, it is specific
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
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
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
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