Development of Synchrotron Footprinting at NSLS and NSLS-II.
NSLS
NSLS-II
Synchrotron
XFP
beamline
footprinting
radiolysis
x-ray.
Journal
Protein and peptide letters
ISSN: 1875-5305
Titre abrégé: Protein Pept Lett
Pays: Netherlands
ID NLM: 9441434
Informations de publication
Date de publication:
2019
2019
Historique:
received:
20
06
2018
revised:
30
10
2018
accepted:
06
11
2018
pubmed:
30
11
2018
medline:
2
3
2019
entrez:
29
11
2018
Statut:
ppublish
Résumé
First developed in the 1990's at the National Synchrotron Light Source, xray synchrotron footprinting is an ideal technique for the analysis of solution-state structure and dynamics of macromolecules. Hydroxyl radicals generated in aqueous samples by intense x-ray beams serve as fine probes of solvent accessibility, rapidly and irreversibly reacting with solvent exposed residues to provide a "snapshot" of the sample state at the time of exposure. Over the last few decades, improvements in instrumentation to expand the technology have continuously pushed the boundaries of biological systems that can be studied using the technique. Dedicated synchrotron beamlines provide important resources for examining fundamental biological mechanisms of folding, ligand binding, catalysis, transcription, translation, and macromolecular assembly. The legacy of synchrotron footprinting at NSLS has led to significant improvement in our understanding of many biological systems, from identifying key structural components in enzymes and transporters to in vivo studies of ribosome assembly. This work continues at the XFP (17-BM) beamline at NSLS-II and facilities at ALS, which are currently accepting proposals for use.
Sections du résumé
BACKGROUND
BACKGROUND
First developed in the 1990's at the National Synchrotron Light Source, xray synchrotron footprinting is an ideal technique for the analysis of solution-state structure and dynamics of macromolecules. Hydroxyl radicals generated in aqueous samples by intense x-ray beams serve as fine probes of solvent accessibility, rapidly and irreversibly reacting with solvent exposed residues to provide a "snapshot" of the sample state at the time of exposure. Over the last few decades, improvements in instrumentation to expand the technology have continuously pushed the boundaries of biological systems that can be studied using the technique.
CONCLUSION
CONCLUSIONS
Dedicated synchrotron beamlines provide important resources for examining fundamental biological mechanisms of folding, ligand binding, catalysis, transcription, translation, and macromolecular assembly. The legacy of synchrotron footprinting at NSLS has led to significant improvement in our understanding of many biological systems, from identifying key structural components in enzymes and transporters to in vivo studies of ribosome assembly. This work continues at the XFP (17-BM) beamline at NSLS-II and facilities at ALS, which are currently accepting proposals for use.
Identifiants
pubmed: 30484397
pii: PPL-EPUB-94853
doi: 10.2174/0929866526666181128125125
doi:
Substances chimiques
Proteins
0
Types de publication
Journal Article
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
55-60Informations de copyright
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