Abstract
The extracellular haemoglobin of the polychaete Tylorrhynchus heterochaetus was studied in solution by small-angle X-ray scattering. The following molecular parameters were determined: radius of gyration 10.8±0.2 nm and a maximum intraparticular distance of 29.5±0.5 nm. Models which fit well the experimental data and reflect also the biochemical structure especially the known number of polypeptide chains are presented.
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