ArticleJournal of biomolecular NMR2015
Efficient segmental isotope labeling of multi-domain proteins using Sortase A.
Article in Journal of biomolecular NMR, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 86 citations in OpenAlex.
- How does p53 work? Regulation by the intrinsically disordered domains.Trends in biochemical sciences · 2025Review
- Application of Sortase-Mediated Ligation for the Synthesis of Block Copolymers and Protein-Polymer Conjugates.Macromolecular bioscience · 2025Article
- Efficient Segmental Isotope Labeling of Integral Membrane Proteins for High-Resolution NMR Studies.Journal of the American Chemical Society · 2024Article
- Article
- Three segment ligation of a 104 kDa multi-domain protein by SrtA and OaAEP1.Journal of biomolecular NMR · 2023Article
- Chemical tools for study and modulation of biomolecular phase transitions.Chemical science · 2022Review
- A Chemical Biology Primer for NMR Spectroscopists.Journal of magnetic resonance open · 2022Article
- Challenges in the use of sortase and other peptide ligases for site-specific protein modification.Chemical Society reviews · 2022Review
- Mobile origin-licensing factors confer resistance to conflicts with RNA polymerase.Cell reports · 2022Article
- nightshift: A Python program for plotting simulated NMR spectra from assigned chemical shifts from the Biological Magnetic Resonance Data Bank.Protein science : a publication of the Protein Society · 2022Article
- Segmental and site-specific isotope labelling strategies for structural analysis of posttranslationally modified proteins.RSC chemical biology · 2021Review
- Conserved allosteric ensembles in disordered proteins using TROSY/anti-TROSY RBiophysical journal · 2021Article
- Laboratory evolution of a sortase enzyme that modifies amyloid-β protein.Nature chemical biology · 2021Article
- Sortase-mediated segmental labeling: A method for segmental assignment of intrinsically disordered regions in proteins.PloS one · 2021Article
- Convenient Auto-Processing Vector Based on Bamboo Mosaic Virus for Presentation of Antigens Through Enzymatic Coupling.Frontiers in immunology · 2021Article
- Deuteration Aiming for Neutron Scattering.Biophysics and physicobiology · 2021Article
- Micellar TIA1 with folded RNA binding domains as a model for reversible stress granule formation.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Deciphering protein post-translational modifications using chemical biology tools.Nature reviews. Chemistry · 2020Review
- Efficient Sortase-Mediated Ligation Using a Common C-Terminal Fusion Tag.Bioconjugate chemistry · 2020Article
- Combining molecular dynamics simulations with small-angle X-ray and neutron scattering data to study multi-domain proteins in solution.PLoS computational biology · 2020Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
NMR studies of multi-domain protein complexes provide unique insight into their molecular interactions and dynamics in solution. For large proteins domain-selective isotope labeling is desired to reduce signal overlap, but available methods require extensive optimization and often give poor ligation yields. We present an optimized strategy for segmental labeling of multi-domain proteins using the S. aureus transpeptidase Sortase A. Critical improvements compared to existing protocols are (1) the efficient removal of cleaved peptide fragments by centrifugal filtration and (2) a strategic design of cleavable and non-cleavable affinity tags for purification. Our approach enables routine production of milligram amounts of purified segmentally labeled protein for NMR and other biophysical studies.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.