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Lysozyme neutron scattering experiments

Neutron experiments were first made on haemoglobin [98,99,147,166,167] and were extended to myoglobin [44,168], lysozyme [169] and catalase [170] as models of typical globular proteins. In parallel with X-ray scattering, the haemoglobin work (mainly in H20) identified a conformational change between the oxy- and deoxy-forms which was reflected in an difference of 0.054 nm in H20 buffers. Scattering curve comparisons to <2 = 3 nm with the crystal structures verified this. [Pg.208]


See other pages where Lysozyme neutron scattering experiments is mentioned: [Pg.125]    [Pg.206]    [Pg.266]    [Pg.112]    [Pg.195]    [Pg.136]    [Pg.142]    [Pg.193]    [Pg.290]    [Pg.159]   
See also in sourсe #XX -- [ Pg.125 ]




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