High Throughput Characterization of Structural Differences Between Closely Related Proteins in Solution
Document Type
Article
Publication Date
2013
Keywords
Partitioning, Protein Structure, Aqueous Two-phase System, Structural Changesolvent Interaction Analysis
Digital Object Identifier (DOI)
https://doi.org/10.1016/j.bbapap.2012.11.004
Abstract
Partitioning of a protein in an aqueous two-phase system (ATPS) is governed by interactions of the protein with aqueous media in the two phases. Here we describe how partitioning of proteins in a set of ATPS of different compositions can be used to quantify differences between 3D structures of closely related proteins. We also provide perspective on practical applications of the technology when comparative analysis of the higher-order structure of proteins is desired.
Was this content written or created while at USF?
Yes
Citation / Publisher Attribution
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, v. 1834, issue 2, p. 583-592
Scholar Commons Citation
Zaslavsky, Alexander; Madeira, Pedro P.; Breydo, Leonid; Uversky, Vladimir N.; Chait, Arnon; and Zaslavsky, Boris Y., "High Throughput Characterization of Structural Differences Between Closely Related Proteins in Solution" (2013). Molecular Medicine Faculty Publications. 517.
https://digitalcommons.usf.edu/mme_facpub/517
