Small angle x-ray scattering dealing with flexible/multidomain protein structures
The use of Small-angle X-ray scattering (SAXS) as a technique to obtain the structural properties of a full length protein having a potential for guiding homology modeling of multidomain one. Furthermore, SAXS is used to detect and quantify the protein flexibility, and as well as to validate structural models with such flexibility.
Many proteins are composed of several domains that pack together into a complex tertiary structure. Multidomain proteins can be challenging for protein structure modeling, particularly those for which templates can be found for individual domains but not for the entire sequence. In such cases, homology modeling and/or crystallography can generate high quality models of the domains but not for the orientations between domains. Small-angle X-ray scattering (SAXS) reports the structural properties of entire proteins and has the potential for guiding homology modeling of multidomain proteins. Furthermore, SAXS is used to detect and quantify the protein flexibility, and as well as to validate structural models with such flexibility.
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