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Reactions with amino and carboxyl groups. Biochemistry d, 1030-1036 (1965 ). 103. Steere, R. , and G. K. Ackers: Restricted diffusion chromatography through calibrated columns of granulated agar gel; a simple method for particle-size determination. Nature 196, 475-476 (1962). 104. Stouffer, J. , and J . A. : The reversible masking of the lysine residue in ~-melanocyte stimulating hormone. Biochim. Biophys. Acta 104, 214--217 (1965). ]05. Swan, J . : Nature 180, 643 (1957) e n t n o m m e n aus Bailey (8).

The SH marks the position of the reactiw~ cvsteine residue in the ~-chain Both types of polypeptide chain in haemoglobin have a very similar three-dimensional conformation to that of the single polypeptide chain of sperrrl whale myoglot~in except for certain deletions. Myoglobin has a inolecular weight of about 17,000. It consists of a single polypeptide chain 153 residues long and one haem group. 4 ,~. resolution (Kendre~e' et al, unpublished work, 21, 22) and it was possible to determine much of the primary sequence from the results of the X-ray analysis.

These lie ill the helical regions G, have no contact with tile haem groups and are buried inside the molecule. Prolinc cannot form part of an x-helix. Myoglobin contains four prolines and all of these occur at corners or in non-helical regions. Ilowevcr, proline is not essential for a corner to be present. A corner m a y contain a proline in one of tile haemoglobin chains but not in myoglobin and vice versa. Also they do not occur in the same places in the two haemoglobin chains. The corners which do not contain a proline residue are stabilized by various means invol;,ing hydrogen bonds between a residue in the corner and one in sonle other part of the chain.

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