Methods to Study the Effect of Solution Variables on the Conformational Dynamics of Intrinsically Disordered Proteins
Document Type
Book Chapter
Publication Date
2022
Digital Object Identifier (DOI)
https://doi.org/10.1016/B978-0-323-90264-9.00033-7
Abstract
Amyloid-β is an intrinsically disordered protein (IDP) that is at the center of Alzheimer's disease (AD). IDPs do not adopt stable three-dimensional structures but exist as highly dynamic ensembles of conformations, and behavior of these ensembles of structures is dramatically affected by the peculiarities of the environment, including different solution variables. Therefore, there is an urgent requirement for enhancing these studies on quasi in vivo conditions, where amyloid formation is impacted by a myriad of solution variables and biochemical interactions. Such studies can further help in finding more efficient treatments for AD. Computational studies complement experiments and provide insights into the impacts of solution variables on IDPs. The aim of this chapter is to introduce the theoretical and computational methods and protocols for studying the impacts of solution variables on a model IDP, amyloid-β.
Was this content written or created while at USF?
Yes
Citation / Publisher Attribution
Methods to Study the Effect of Solution Variables on the Conformational Dynamics of Intrinsically Disordered Proteins, in T. Tripathi & V. K. Dubey (Eds.), Advances in Protein Molecular and Structural Biology Methods, Academic Press, p. 551-563
Scholar Commons Citation
Alici, Hakan; Hasekioglu, Orkun; Uversky, Vladimir N.; and Coskuner-Weber, Orkid, "Methods to Study the Effect of Solution Variables on the Conformational Dynamics of Intrinsically Disordered Proteins" (2022). Molecular Medicine Faculty Publications. 1138.
https://digitalcommons.usf.edu/mme_facpub/1138
