Section 8 - Amino Acids, Proteins and DNA Flashcards
What makes amino acids amphoteric?
They have a basic amino group (NH2) and an acidic carboxyl group (COOH).
What kind of isomerism do amino acids display?
Optical - they have a chiral carbon.
Which amino acid does not display isomerism?
Glycine - its R group is another hydrogen/
What is a zwitterion?
A dipolar ion - it has a positive and negative charge in different parts of the molecule.
What is the isolectric point?
The pH when the average overall charge of the amino acid is zero.
What is a suitable way to identify unknown amino acids?
Thin-layer chromatography.
What is the name for condensation polymers of amino acids?
Proteins
What is the link in a protein chain?
Peptide link
What are the conditions for hydrolysis of proteins?
- hot aqueous 6M HCl acid
- heat
- reflux
- 24 hours
What is the primary structure of a protein?
The sequence of amino acids in the polypeptide chain.
What is the secondary structure of a protein?
The shape of the chain - the peptide links form hydrpgen bonds creating either an alpha helix (spiral) or beta-pleated (folded) sheet.
What is the tertiary structure of a protein?
The extra bonds formed between different parts of the polypeptide chain, which gives the protein a 3-dimensional shape.
Which types of bonds help to keep proteins in shape?
Hydrogen and Disulfide bonds.
How do hydrogen bonds form in proteins?
They exist between the -OH and -NH2 groups.
How do disulfide bonds form in proteins?
Cysteine contains a thiol group (-SH). These can lose their H atoms and join together forming a disulfide bond, linking together parts of the protein chain.
Which factors can affect the formation of hydrogen and disulfide bonds?
- temperature
- pH
Define enzymes
Biological catalysts which speed up chemical reactions
What type of reactions do enzymes catalyse in the human body?
Metablolic reactions
What is an active site?
The area on an enzyme that the substrate fits into so that it can interact with the molecule.
Why are enzymes stereospecific and what does this mean?
They have chiral centres and only one enantiomer of a substrate will fit into the active site.
What is an inhibitor?
A molecule which has a similar shape to the substrate which bonds to the active site but doesn’t react - just blocks the substrate from getting in.
What is the amount of enzyme inhibition affected by?
- how strongly the the inhibitor bonds to the active site
- the relative concentrations of inhibitor and substrate
How do inhibiting drugs work?
- block active site of enzyme and stop it working
- eg. some antibiotics block the active site of enzymes in bacteria which make their cell walls so that eventually they burst.
Why is it a problem if inhibiting drugs are chiral?
Active sites of enzymes are stereospecific