Biomaterial Database

Structure of Helix pomatia oxy-beta-hemocyanin and deoxy-beta-hemocyanin tubular polymers. 1979

J F Van Breemen, and J H Ploegman, and E F Van Bruggen

Mild trypsinolysis of Helix pomatia beta-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--135]. 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.

UI	MeSH Term	Description	Entries
D008854	Microscopy, Electron	Microscopy using an electron beam, instead of light, to visualize the sample, thereby allowing much greater magnification. The interactions of ELECTRONS with specimens are used to provide information about the fine structure of that specimen. In TRANSMISSION ELECTRON MICROSCOPY the reactions of the electrons that are transmitted through the specimen are imaged. In SCANNING ELECTRON MICROSCOPY an electron beam falls at a non-normal angle on the specimen and the image is derived from the reactions occurring above the plane of the specimen.	Electron Microscopy
D010100	Oxygen	An element with atomic symbol O, atomic number 8, and atomic weight [15.99903; 15.99977]. It is the most abundant element on earth and essential for respiration.	Dioxygen,Oxygen-16,Oxygen 16
D011487	Protein Conformation	The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).	Conformation, Protein,Conformations, Protein,Protein Conformations
D006372	Helix, Snails	A genus of chiefly Eurasian and African land snails including the principal edible snails as well as several pests of cultivated plants.	Helix (Snails),Snails Helix
D006433	Hemocyanins	Metalloproteins that function as oxygen transport proteins in the HEMOLYMPH of MOLLUSKS and ARTHROPODS. They are characterized by two copper atoms, coordinated with HISTIDINE residues, that reversibly bind a single oxygen molecule; they do not contain HEME groups.	Hemocyanin,alpha-Haemocyanin,alpha-Hemocyanin,alpha-Hemocyanins,alpha Haemocyanin,alpha Hemocyanin,alpha Hemocyanins
D000818	Animals	Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA.	Animal,Metazoa,Animalia
D046911	Macromolecular Substances	Compounds and molecular complexes that consist of very large numbers of atoms and are generally over 500 kDa in size. In biological systems macromolecular substances usually can be visualized using ELECTRON MICROSCOPY and are distinguished from ORGANELLES by the lack of a membrane structure.	Macromolecular Complexes,Macromolecular Compounds,Macromolecular Compounds and Complexes,Complexes, Macromolecular,Compounds, Macromolecular,Substances, Macromolecular