Measuring translational diffusion of (15)N-enriched biomolecules in complex solutions with a simplified (1)H-(15)N HMQC-filtered BEST sequence
Journal Title
European Biophys Journal
Publication Type
Journal Article in press
Abstract
Pulsed-field gradient nuclear magnetic resonance has seen an increase in applications spanning a broad range of disciplines where molecular translational diffusion properties are of interest. The current study introduces and experimentally evaluates the measurement of translational diffusion coefficients of (15)N-enriched biomolecules using a (1)H-(15)N HMQC-filtered band-selective excitation short transient (BEST) sequence as an alternative to the previously described SOFAST-XSTE sequence. The results demonstrate that accurate translational diffusion coefficients of (15)N-labelled peptides and proteins can be obtained using this alternative (1)H-(15)N HMQC-filtered BEST sequence which is implementable on NMR spectrometers equipped with probes fitted with a single-axis field gradient, including most cryoprobes dedicated to bio-NMR. The sequence is of potential use for direct quantification of protein or peptide translational diffusion within complex systems, such as in mixtures of macromolecules, crowded solutions, membrane-mimicking media and in bicontinuous cubic phases, where conventional sequences may not be readily applicable due to the presence of intense signals arising from sources other than the protein or peptide under investigation.
Publisher
Springer
Research Division(s)
Structural Biology
PubMed ID
29785510
Terms of Use/Rights Notice
Refer to copyright notice on published article.


Creation Date: 2018-05-31 09:17:48
Last Modified: 2018-05-31 09:39:37
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