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Structural characterization of high-protein system through ultra-small and small-angle X-ray scattering

Journal Article · · Current Opinion in Food Science
 [1];  [2]
  1. Purdue Univ., West Lafayette, IN (United States)
  2. 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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