Table 1::Comparison of structural features between Oxy/Deoxy Hb

Table 1

Comparison of structural features between Oxy/Deoxy Hb

	Deoxy (1hv4)	Oxy (1a4f)
α-chain
No. residues	141	141
Strands	0	0
α-helices	6 (69.5%)*	7 (66%)
3₁₀ helices	2 (5.7%)*	1 (4.3%)
2° Struct	HHGTTHTHTHTHG	HTHGTTHTHHTHTHTT
β-chain
No. residues	146	146
Strands	0	0
α-helices	7 (70.5%)	7 (68.5%)
3₁₀ helices	2 (8.9%)	2 (8.2%)
2° Struct	HHGHHTHTHGHT	HTHGHHTHHGHT

Deoxy: http://www.ebi.ac.uk/thornton-srv/databases/pdbsum/1hv4/main.html

Oxy: http://www.ebi.ac.uk/thornton-srv/databases/pdbsum/1a4f/main.html

Overall: 68.25% α-helix (i→i+4), 6.775% 3₁₀-helix (i→i+3).

*Note, the data in the shaded columns are most likely anomalous due to the relatively low resolution of the structure of the deoxy haemoglobin (2.80Å for 1vh4) vs. 2Å for the oxy haemoglobin (1a4f) as other deoxy haemoglobins (e.g., human adult, 2hhb; human foetal, 1fdh; P.bernacchii, 1hbh, etc.) showed no changes in the overall protein fold.