Abstract
In order to understand the molecular mechanism of a protein function, it is important to reveal the conformational change of the protein during functioning. Time-resolved X-ray crystallography has been utilized to reveal the structural change during functioning, and has revealed the local structural change after triggering. However, global conformational changes which are demonstrated by solution studies with various spectroscopic measurements are generally difficult to observe through time-resolved crystallography. Furthermore, the structural properties of folding intermediates cannot be revealed by crystallography. Solution X-ray scattering (SOXS) is one of the powerful techniques to study solution structure of a protein and its change. We will describe the solution structure analysis of the pho-tointermediate of a light-absorbing protein by high-angle solution X-ray scattering.
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