Small-angle X-ray scattering (SAXS) is a structural characterization method applicable to biological macromolecules in solution. The great advantage of solution scattering is that the systems can be investigated in near-physiological conditions and their response to external changes can also be easily investigated. In this chapter, we discuss the application of SAXS for studying the conformation of helicases alone and in complex with other biological macromolecules. The DEAD-box helicase eIF4A and the DEAH/RHA helicase Prp43 are investigated for their solution structures, and the analysis of the collected scattering data is presented. A wide range of methods for analysis of SAXS data are presented and discussed. Ab initio methods can be used to yield low-resolution solution structures, and when models with atomic resolution are available, these can be included to aid the determination of solution structures. Using such prior information relating to the systems studied and applying a variety of methods, substantial insight can be gained about solution structures and interactions of biological macromolecules through small-angle scattering.
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http://dx.doi.org/10.1016/B978-0-12-396546-2.00031-0 | DOI Listing |
J Chem Inf Model
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Donostia International Physics Center (DIPC), 20018 Donostia-San Sebastián, Spain.
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January 2025
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January 2025
National Key Laboratory of Oil and Gas Reservoir Geology and Exploitation, Southwest Petroleum University, Chengdu 610500, P. R. China.
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January 2025
Center for Molecular Spectroscopy and Dynamics, Institute for Basic Science, Seoul 02841, Korea.
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View Article and Find Full Text PDFBiochem Mol Biol Educ
January 2025
Department of Chemistry and Biochemistry, Miami University, Oxford, Ohio, USA.
We created a novel laboratory experience where undergraduate students explore the techniques used to study protein misfolding, unfolding, and aggregation. Despite the importance of protein misfolding and aggregation diseases, protein unfolding is not typically explored in undergraduate biochemistry laboratory classes. Yeast alcohol dehydrogenase (YADH) is used in the undergraduate biochemistry laboratory course at Miami University as the model system to explore protein overexpression and purification, bioinformatics, and enzyme characterization.
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