Structure of Helix pomatia Oxy‐β‐hemocyanin and Deoxy‐β‐hemocyanin Tubular Polymers

• Published in: European journal of biochemistry Vol. 100; no. 1; pp. 61 - 65
• Main Authors: BREEMEN, Jan F. L., PLOEGMAN, Jan H., BRUGGEN, Ernst F. J.
• Format: Journal Article
• Language: English
• Published: Oxford, UK Blackwell Publishing Ltd 01.10.1979
• Subjects: Animals; Helix (Snails) - analysis; Hemocyanins; Macromolecular Substances; Microscopy, Electron; Oxygen; Protein Conformation
• ISSN: 0014-2956; 1432-1033
• DOI: 10.1111/j.1432-1033.1979.tb02033.x

Mild trypsinolysis of Helix pomatiaβ‐hemocyanin leads to the formation of tubular polymers after removal of the collar part [van Breemen, J. F. L., Wichertjes, T., Muller, M. F. J., van Driel, R., and van Bruggen, E. F. J. (1975) Eur. J. Biochem. 60, 129–1351]. Three‐dimensional image reconstruction from electron micrographs of negatively stained tubular polymers showed: (a) alternating deep and shallow grooves in between the 10 helical chains, (b) the presence and position of two domains within each morphological wall‐unit of the Mellema and Klug model [Mellema, J. E. and Klug, A. (1972) Nature (Lond.) 239, 146–150]. Optical diffraction of oxy and deoxygenated tubular polymers indicate a significant decrease in diameter with a concomitant increase in length upon deoxygenation.