TitleThe structure & function of haemoglobin (hemoglobin)
CreditsHuehns, E. R.; May, Alison
PublisherUniversity of London
|Deprecated CHM identification number||102624818_V|
Copyright HolderU. of London
DescriptionA computer-generated 3-D anaglyph film, made in collaboration with the Stichting Film en Wetenschap, Utrecht. Script by Professor E. R. Huehns, University College Hospital, London, and Dr Alison May, University Hospital of Wales, Cardiff.
Based on the work of M. F. Perutz and his coworkers, MRC Laboratories of Molecular Biology, Cambridge.
By means of computer-drawn stereo pairs which, when viewed through the red/green spectacles, appear as 3-D ball-and-stick models of the molecule, the current mechanism by which haemoglobin binds and releases oxygen is explained. By working outwards from one iron atom in its haem group, and building the molecule stage by stage, the roles of several of the individual amino-acid residues are illustrated. The two types of subunit, and the two forms of subunit contact, are examined and the change in conformation on going from the oxy- to the deoxy- structure is shown in some detail. The co-operativity exhibited by the subunits within the whole molecule is illustrated by the formation and breaking of salt bridges.
00 How the anaglyph system works.
02 The whole molecule illstrated by just the α - carbon atoms and haems.
04 The haem group.
06 The haem pocket.
10 Oxy- deoxy- transitions in α1 subunit.
13 The second (β1) subunit.
15 The α1 - β1 contact.
16 The two dimers.
17 The α1 - β1 contact.
20 The salt bridges.
22 The oxygenation and deoxygenation of the whole molecule.
CDC 7600 output is plotted on a CalComp 1670. Includes 7 pairs of 3-D glasses.