Lecture notes
Haemoglobin
- Module
- Medicine
- Institution
- Queens University Belfast (QUB)
Lecture notes of 7 pages for the course Medicine at QUB (Physiology)
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cHAEMOGLOBIN
1213C are biconcave to provide a
surface for and
large area uptake
release of O2 and CO2
Erythrocyte function
02 transport depends on j
Hb in erythrocytes
Tetramer of 4 protein chains
the globins each with a harem
group porphyrinring with central Feat
HbA Adult Hb has 2 alpha and 2 beta chains plus haem
groups
The shape of a protein is determined by its amino acid
sequence
20 types of amino acid used in proteins linked
by peptid
bonds t side chain
Chemical properties of component amino acids dictate
, the shape of the protein and its properties
Structure relates to function
Proteins fold into confirmations of lowest energy
Con formation Proteins final folded shape
Achieving the correct shape depends on thermodynamics
other proteins known as molecular chaperones These
make the process efficient and reliable
4 levels of protein structure
4 Hydrophobic forces help
f old proteins into compac
con formations
3 types of non covalent
bonding influences folding
Primary structure
The gene coding for a
given protein is co linear with
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