Dissertation in Draft: Chapter X

Date:
1952-1953
Reference:
PP/CRI/F/1/10
Catalogue details

Licence: In copyright

Credit: Dissertation in Draft: Chapter X. Source: Wellcome Collection.

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    Reprinted from Acta Crystallographica^Y ol. 5, Part 3, May 1952 PRINTED II C/L&Jp&sr X Aet€h-Grg«tTii%Styr~S~,SSt The Height of the Vector Rods in the Three-Dimensional Patterson of Haemoglobin By F. H. C. Crick The Medical Research Council Unit for the Study of the Molecular Structure of Biological Systems, Cavendish laboratory, Cambridge, England (Received 15 November 1951) A method is described for calculating the average height of the vector rods in the three-dimensional Patterson of haemoglobin. The calculations have been carried out for the a-helix. They show that the simple models previously considered for haemoglobin give peaks which are too high, and that to obtain even rough agreepaént either less than about half the protein must be put into chains parallel to the X axis'or considerable irregularity must be introduced. The evidence suggests -that theJolded polypeptide chain does not run in one direction for n * e „than 20 Â at a stretch. J. Introduction The three-dimensional Patterson synthesis of horse methaemoglobin has, as one of its features, rod-shaped regions of high vector density, parallel to the X axis, which Perutz (1949) interpreted in terms of straight rods of high electron density in the molecule; he suggested that these rods,were due to folded poly peptide chains arranged in hexagonal close packing
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