Q) Explain the structural adaptation of haemoglobin to its function
Main points | |
Key idea: | Function and properties of haemoglobin |
· Fn: transports O2 via the rbc to respiring cells, tissues · Properties: compact, having high O2 carrying capacity, soluble in water | |
Key idea: | Folding of each subunit polypeptide makes protein soluble in water (blood) |
· Ref to protein comprising of 4 polypep subunits (2α, 2β) to form a compact globular protein w quaternary struc · Ref to each subunit polypep chain folds extensively upon itself to form a compact, globular struc - folding leads to distribution of diff aa w/n struc · Non-polar aa residues at interior of struc · Hydrophilic R groups of polar aa residues point outward toward aq medium, interact w water mol | |
Key idea: | Each haemoglobin can carry up to 4 O2 molecules |
· Each polypep contains a haem (or heme) gp, held in place w/n folded polypep by weak bonds b/w haem & side chains of some aa residues of polypep · Ref to haem gp comprises of a flat porphyrin ring containing Fe2+ that binds reversibly to an O2 to form oxyhaemoglobin · Ref to each Hb (w 4 polypep subunits), can carry up to 4 O2 at a time | |
Key idea: | Compact nature of haemoglobin allows many to be packed in each red blood cell |
· Ref to transporting O2 more efficient | |
Comments: (i) Visualize the answer with the aid of a labelled diagram. (ii) Verbalize the answer + write down the main points w/o referring to the answer (use abbreviations) (iii) Read again within the next 24h & once more within 72h (do not spend more than 10min) | |
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