The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
NMR as a readout to monitor and restore the integrity of complex chemoenzymatic reactions
Open accessPreprint — published as 10.1016/j.jmr.2022.107265 · Paper page
Abstract
The non-invasive nature of NMR offers a means to monitor biochemical reactions in situ at the atomic-level. We harness this advantage to monitor a complex chemoenzymatic reaction that sequentially modifies reagents and loads the product on a nonribosomal peptide synthetase carrier protein. We present a protocol including a novel pulse sequence that permits to assess both the integrity of reagents and the completion of each step in the reaction, thus alleviating otherwise time-consuming and costly approaches to debug and repeat inefficient reactions. This study highlights the importance of NMR as a tool to establish reliable and reproducible experimental conditions in biochemical studies. Graphical Abstract:
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764
Flagged first, then by citations
Research works printed but not linked: 40
- 10.1038/s41586-020-2829-0 · DOI
- 10.1016/j.mib.2019.10.007 · DOI
- 10.1146/annurev.micro.58.030603.123615 · DOI
- 2017, Nonribosomal Peptide Synthesis—Principles and Prospects, Angew, Chemie - Int, 56, 3770, 10.1002/anie.201609079 · DOI
- J.M. Reimer , M. Eivaskhani , I. Harb , A. Guarné , M. Weigt , T. Martin Schmeing , Structures of a dimodular nonribosomal peptide synthetase reveal conformational flexibility, Science (80-.). 366 (2019). https://doi.org/10.1126/science.aaw4388. · DOI
- 10.1038/s41467-020-20241-w · DOI · Paper page
- 10.1016/j.str.2017.03.014 · DOI
- 10.1021/jacs.5b07772 · DOI
- 10.1021/jacs.5b04525 · DOI
- 10.1039/b512735a · DOI
- 2018, An enhanced chemoenzymatic method for loading substrates onto carrier protein domains, Biochem, Cell Biol, 96, 372
- 2004, One-pot chemoenzymatic preparation of coenzyme A analogues, Anal. Biochem, 324, 100, 10.1016/j.ab.2003.09.005 · DOI
- 10.1016/S1074-5521(96)90181-7 · DOI
- 2009, Crosslinking Studies of Protein-Protein Interactions in Nonribosomal Peptide Biosynthesis, Chem. Biol, 16, 372, 10.1016/j.chembiol.2009.02.009 · DOI
- 10.1074/jbc.M116.766220 · DOI
- 10.1039/C3SC53154F · DOI
- 10.1021/ja902464v · DOI
- 10.1128/JB.00732-07 · DOI
- 10.1074/jbc.274.38.27105 · DOI
- 2010, Creating cellulose-binding domain fusions of the coenzymea biosynthetic enzymes to enable reactor-based biotransformations, ChemCatChem, 2, 1239, 10.1002/cctc.201000197 · DOI
- 10.1002/cctc.201000139 · DOI
- 10.1021/bi9812571 · DOI
- 2021, Using delayed decoupling to attenuate residual signals in editing filters, Magn. Reson, 2, 475, 10.5194/mr-2-475-2021 · DOI
- 10.1016/S0079-6565(00)00020-0 · DOI
- 10.1016/0022-2364(92)90304-P · DOI
- 10.1016/S1090-7807(02)00176-3 · DOI
- 10.1063/1.1695690 · DOI
- 10.1063/1.1673336 · DOI
- 10.1016/S0079-6565(99)00003-5 · DOI
- 10.1006/jmre.1997.1376 · DOI
- 10.1006/jmra.1995.1176 · DOI
- 2014, Measuring translational diffusion coefficients of peptides and proteins by pfg-nmr using band-selective rf pulses, Eur. Biophys. J, 43, 331, 10.1007/s00249-014-0965-x · DOI
- 1993, Experimental aspects of chirp NMR spectroscopy, J. Magn. Reson. - Ser. A, 102, 293, 10.1006/jmra.1993.1107 · DOI
- 10.1016/0022-2364(85)90122-2 · DOI
- 10.1038/nprot.2006.43 · DOI
- 10.1021/ja063217n · DOI
- 10.1080/00268978900102331 · DOI
- 2009, HMDB: A knowledgebase for the human metabolome, Nucleic Acids Res, 37, 603, 10.1093/nar/gkn810 · DOI
- 2019, Extending the Scope of 1 H NMR Spectroscopy for the Analysis of Cellular, Anal. Chem, 91, 2464, 10.1021/acs.analchem.8b05286 · DOI
- 2017, Unique identifiers for small molecules enable rigorous labeling of their atoms, Sci. Data, 4, 1
Metadata
- Authors
- Marincin, K. A., Hwang, Y., Kengmana, E. S., Meyers, D. J., & Frueh, D. P.
- Affiliations
- Johns Hopkins University (US)
- Corresponding author
- Frueh, Dominique P.
- Venue
- Journal of Magnetic Resonance
- Publisher
- openRxiv
- Published
- 2022-05-14
- Volume
- 342
- Pages
- 107265-107265
- ISSN
- 1090-7807 (ISSN-L)
- PMC
- PMC9463103
- OpenAlex
- W4284881971
- Cited by
- 0
- References
- 1
- FWCI
- 0.00
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Journal of Magnetic Resonance (acceptedVersion)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Flight Attendant Medical Research Institute
- Institute for Clinical and Translational Research, University of Maryland, Baltimore
- National Institutes of Health (UL1TR003098)
- National Institute of General Medical Sciences (R01GM104257, T32GM080189, T32GM149382)
- National Center for Advancing Translational Sciences
- Topics
- Physical Sciences › Chemistry › Spectroscopy › Advanced NMR Techniques and Applications
- Life Sciences › Immunology and Microbiology › Applied Microbiology and Biotechnology › Microbial Natural Products and Biosynthesis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolomics and Mass Spectrometry Studies
- Keywords
- chemoenzymatic synthesis, nonribosomal peptide synthetase, NMR pulse sequences, reaction monitoring, in situ NMR, reproducibility, pulse sequence design
- MeSH terms
- Magnetic Resonance Imaging, Magnetic Resonance Spectroscopy
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review