Distance calculation of residues neighbouring to lysozyme antigenic sites. Site-neighbouring residues whose evolutionary substitution can modify the characteristics and binding energy of the sites

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Abstract
By using the antigenic structure of [hen] lysozyme and the X-ray co-ordinates the closest-atom distances between each of the residues in the 3 antigenic sites and all the other amino acids of the lysozyme molecule were calculated. These calculations enabled us to identify the nearest neighbors to each of the site residues. The immediate environment of each site residue is described. For the 3 antigenic sites there are 71 neighboring residues. The effects of evolutionary amino acid substitutions in site-neighboring residues on the binding capacity of protein binding sites in general and on protein antigenic sites in particular are discussed. These, together with the direct replacements in site residues, will account for the major effects. The limitations of this treatment are stressed. The smaller effects on antigenic sites of replacements at once-removed and even more distant locations, which, when they become cumulative, could be considerable, are brought to attention together with any influences of conformational readjustments that can take place as a result of evolutionary amino acid replacements.

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