Structural characterization of high-protein system through ultra-small and small-angle X-ray scattering
Journal Article
·
· Current Opinion in Food Science
- Purdue Univ., West Lafayette, IN (United States)
- Argonne National Laboratory (ANL), Argonne, IL (United States)
High-protein systems exhibit a hierarchical structure consisting of interconnected multiscale length assemblies. Recent investigations are directed toward identifying these structural units under various processing and environmental conditions to establish structure–function correlations. Ultra-small and small-angle X-ray scattering (USAXS/SAXS) has become a crucial tool for characterizing the structures of proteins and their clusters/aggregates, ranging from nanometers to micrometers, with minimal disruption to their original state. Here, this review first describes the facilities and principles of X-ray scattering, followed by discussions on the analysis of scattering data, including the interpretation of fitting models. It then delves into the main applications of USAXS/SAXS in plant and dairy protein-rich systems. Future strategies to enhance the utilization of scattering techniques for elucidating the structure of high-protein systems are also included.
- Research Organization:
- Argonne National Laboratory (ANL), Argonne, IL (United States)
- Sponsoring Organization:
- USDOE Office of Science (SC), Basic Energy Sciences (BES). Scientific User Facilities (SUF)
- Grant/Contract Number:
- AC02-06CH11357
- OSTI ID:
- 2433818
- Journal Information:
- Current Opinion in Food Science, Journal Name: Current Opinion in Food Science Vol. 59; ISSN 2214-7993
- Publisher:
- ElsevierCopyright Statement
- Country of Publication:
- United States
- Language:
- English
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