By George A. F. Roberts (auth.)
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Further doubt arises from the fact that this 40 CHITIN CHEMISTRY adsorbed protein could be removed by extraction at pH = 9, which is not the case with the normal protein residues on chitin. 16) link, which in the case of the former would require involvement of a C-terminal histidine residue while the aspartic acid residue could be located in any position in the protein chain. 18). Such a mode of attachment would mean that only one protein chain could be attached to each chitin chain, the point of attachment being the terminal reducing sugar unit.
1 Introduction Chitin has a highly ordered, crystalline structure as evidenced by X-ray diffraction studies. It has been found in three polymorphic forms, a-, ~ and y-chitin,82 which differ in the arrangement of the chains within the crystalline regions. In a-chitin the chains are anti-parallel, in ~-chitin they are parallel, and in y-chitin two chains are 'up' to each chain 'down'82 (Figure 1. 7) . 7 j3-chitin y-chitin Arrangement of the polymer chains in the three forms of chitin 22 CHITIN CHEMISTRY The most abundant form is a-chitin, which also appears to be the most stable since both the ~- and y-chitin may be converted into the a-form by suitable treatments.
11. The unit cell contains disaccharide sections of two chains with full intramolecular C(3')-OH ... 0(5) and intermolecular C(21)N-H ... 0=C(73) hydrogen bonding and a 50150 statistical mixture of 0(6/)H. 0(71) 1 O(62)H ... 0(6/) and 0(62)H ... 0(72') 1 0(6/)H ... 0(62) intra-I intermolecular pairs of hydrogen bonds. The intramolecular CH20H ... H O=C and intermolecular CH20H ... 79 A respectively, while the intermolecular N-H ... 73 A. This model answers the criticisms of the Carlstrom model listed above.