open access

https://hdl.handle.net/2115/94011

Conformational Distribution of a Multi-domain Protein Measured by Single-Pair Small Angle X-ray Scattering

英語

2024-01-25

American Chemical Society

Journal of physical chemistry letters

15(3)

744-750

The difficulty in evaluating the conformational distribution of proteins in solution often hinders mechanistic insights. One possible strategy for visualizing conformational distribution is distance distribution measurement by single-pair small-angle X-ray scattering (SAXS), in which the scattering interference from only a specific pair of atoms in the target molecule is extracted. Despite this promising concept, with few applications in synthetic small molecules and DNA, technical difficulties have prevented its application in protein conformational studies. This study used a synthetic tag to fix the lanthanide ion at desired sites on the protein and used single-pair SAXS with contrast matching to evaluate the conformational distribution of the multidomain protein enzyme MurD. These data highlighted the broad conformational and ligand-driven distribution shifts of MurD in solution. This study proposes an important strategy in solution structural biology that targets dynamic proteins, including multidomain and intrinsically disordered proteins.

学術雑誌論文

Accepted Manuscript

This document is the Accepted Manuscript version of a Published Work that appeared in final form in Journal of physical chemistry letters, copyright ©2024 American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see http://pubs.acs.org/articlesonrequest/AOR-JIWBPKUEU7JPHT9QMRW9

1948-7185