Heteronuclear NMR spectroscopy of proteins encapsulated in cubic phase lipids
Autor: | David W. Keizer, Thomas G. Meikle, Paul R. Gooley, Frances Separovic, Shenggen Yao, Ashish Sethi, Charlotte E. Conn, Jeffrey J. Babon |
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Rok vydání: | 2019 |
Předmět: |
Nuclear and High Energy Physics
Aqueous solution Nitrogen Isotopes Biophysics Nuclear magnetic resonance spectroscopy 010402 general chemistry Condensed Matter Physics Lipids Sensitivity and Specificity 01 natural sciences Biochemistry Protein tertiary structure 030218 nuclear medicine & medical imaging 0104 chemical sciences Nanomaterials Solvent 03 medical and health sciences Crystallography 0302 clinical medicine Bacterial Proteins Heteronuclear molecule lipids (amino acids peptides and proteins) Spectroscopy Nuclear Magnetic Resonance Biomolecular Heteronuclear single quantum coherence spectroscopy |
Zdroj: | Journal of Magnetic Resonance. 305:146-151 |
ISSN: | 1090-7807 |
DOI: | 10.1016/j.jmr.2019.06.017 |
Popis: | Lipidic cubic phases, which form spontaneously via the self-assembly of certain lipids in an aqueous environment, are highly prospective nanomaterials with applications in membrane protein X-ray crystallography and drug delivery. Here we report 1H-15N heteronuclear single/multiple quantum coherence (HSQC, HMQC) spectra of 15N-enriched proteins encapsulated in inverse bicontinuous lipidic cubic phases obtained on a standard commercial high resolution NMR spectrometer at ambient temperature. 15N-enriched proteins encapsulated in this lipidic cubic phase show: (i) no significant changes in tertiary structure, (ii) significantly reduced solvent chemical exchange of backbone amides, which potentially provides a novel concept for quantifying residue-specific hydration; and (iii) improved spectral sensitivity achieved with band-selective excitation short-transient (BEST) spectroscopy, which is attributed to the presence of an abundant source of 1H nuclear spins originating from the lipid component of the cubic phase. |
Databáze: | OpenAIRE |
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