Structure of the pigeon lysozyme and its relationship with other type c lysozymes.
作者： Rosalía Rodríguez , Luis Menéndez-Arias , Gonzalo Gonzalez de Buitrago , JoséG. Gavilanes
DOI: 10.1016/0305-0491(87)90245-8
关键词: Antigenicity 、 Lysozyme 、 Egg white 、 Protein secondary structure 、 Protein tertiary structure 、 Enzyme 、 Muramidase 、 Crystallography 、 Biology 、 Protein structure
摘要: 1. The secondary structure of the pigeon egg-white lysozyme shows important differences when compared to other type c lysozymes. These are mainly located at region comprising residues 77-84. This segment contains one alpha-helix in lysozymes studied by means an X-ray analysis, while such positions would form two beta-bends. 2. Analysis tertiary hydropathy profiles reveals that above seems be more hydrophilic enzyme than 3. Though a certain similarity calcium-binding loop alpha-lactalbumins is detected lysozyme, circular dichroism spectra protein neutral pH do not change presence Ca2+ ions. 4. presented structural analysis discussed terms function-structure and antigenicity relationships between
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