Session 2-protein structure and affinity Flashcards
what is the name for improper folding of a protein?
amyloidoses
which bonds are involved in the different levels of the protein structure?
primary-covalent peptide
secondary-hydrogen
tertiary-hydrogen,VDW, hydrophobic and philic,disulphide,ionic .
what are they key features of an alpha helix?
- right handed helix
- 3.6 amino acids per turn
- small hydrophobic amino acids like alanine and leucine are strong helix formers
- proline breaks helix due to its arrangements
what are they key features of a beta pleated sheet?
- parallel or anti
- multiple interstrand h bonds
describe myoglobin
- single subunit protein containing one haem group that binds to ONE O2 molecule
- hyperbolic
describe Hb
- 2 alpha and 2 beta subunits
- 4 haem groups with 4 O2s able to bind
- sigmoidal curve
which state of Hb has a high affinity for oxygen and which has a low affinity?(Hbs affinity for O2 increases as more O2 binds)
Relaxed state=high affinity
tense state=low affinity
what effect does BPG have on HB affinity for o2 and why?
- decreases affinity for o2
- BPG increases at high altitudes promoting o2 release at tissues
- produces during metab so o2 is released more readily in high metabolism areas
what effect does co2 and H+ have on o2 affinity?
- decreases affinity
- at sites of low ph and high h+ conc, and increased co2 (e.g. muscle tissue) more o2 released (Bohr)
what is secondary structure?
polypeptide chains that form alpha helices and beta sheets and bonding
what amino acid is substituted in sickle cell anaemia?
glutamate to valine
what are thalassaemias?
group of genetic disorders where there is an imbalance of alpha and beta subunits
which thalassaemias appear before and which appear after birth?
Beta=after birth
alpha=before birth
give an example of a non polar amino acid
glycine
give an example of an uncharged polar molecule
glutamine