Medizinische Universität Graz Austria/Österreich - Forschungsportal - Medical University of Graz
Gewählte Publikation:
SHR Neuro Krebs Kardio Lipid Stoffw Microb
Charlier, C; Courtney, JM; Alderson, TR; Anfinrud, P; Bax, A.
Monitoring 15N Chemical Shifts During Protein Folding by Pressure-Jump NMR.
J Am Chem Soc. 2018; 140(26): 8096-8099.
Doi: 10.1021/jacs.8b04833
[OPEN ACCESS]
Web of Science
PubMed
FullText
FullText_MUG
- Co-Autor*innen der Med Uni Graz
- Alderson Thomas Reid
- Altmetrics:
- Dimensions Citations:
- Plum Analytics:
- Scite (citation analytics):
- Abstract:
- Pressure-jump hardware permits direct observation of protein NMR spectra during a cyclically repeated protein folding process. For a two-state folding protein, the change in resonance frequency will occur nearly instantaneously when the protein clears the transition state barrier, resulting in a monoexponential change of the ensemble-averaged chemical shift. However, protein folding pathways can be more complex and contain metastable intermediates. With a pseudo-3D NMR experiment that utilizes stroboscopic observation, we measure the ensemble-averaged chemical shifts, including those of exchange-broadened intermediates, during the folding process. Such measurements for a pressure-sensitized mutant of ubiquitin show an on-pathway kinetic intermediate whose 15N chemical shifts differ most from the natively folded protein for strands β5, its preceding turn, and the two strands that pair with β5 in the native structure.
- Find related publications in this database (using NLM MeSH Indexing)
- Nitrogen Isotopes - administration & dosage
- Nuclear Magnetic Resonance, Biomolecular - administration & dosage
- Pressure - administration & dosage
- Protein Folding - administration & dosage