ArticleBiopolymers2013
NMR-profiles of protein solutions.
Article in Biopolymers, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 18 citations in OpenAlex.
- Applications and prospects of cryo-EM in drug discovery.Military Medical Research · 2023Review
- Chain-Selective Isotopic Labeling of the Heterodimeric Type III Secretion Chaperone, Scc4:Scc1, Reveals the Total Structural Rearrangement of theBiomolecules · 2020Article
- NMR spectra of PB2 627, the RNA-binding domain in influenza A virus RNA polymerase that contains the pathogenicity factor lysine 627, and improvement of the spectra by small osmolytes.Biochemistry and biophysics reports · 2017Article
- Modern Technologies of Solution Nuclear Magnetic Resonance Spectroscopy for Three-dimensional Structure Determination of Proteins Open Avenues for Life Scientists.Computational and structural biotechnology journal · 2017Review
- NMR in structural genomics to increase structural coverage of the protein universe: Delivered by Prof. Kurt Wüthrich on 7 July 2013 at the 38th FEBS Congress in St. Petersburg, Russia.The FEBS journal · 2016Article
- The acidic domain is a unique structural feature of the splicing factor SYNCRIP.Protein science : a publication of the Protein Society · 2016Article
- Facilitating unambiguous NMR assignments and enabling higher probe density through selective labeling of all methyl containing amino acids.Journal of biomolecular NMR · 2016Article
- Dlx5 Homeodomain:DNA Complex: Structure, Binding and Effect of Mutations Related to Split Hand and Foot Malformation Syndrome.Journal of molecular biology · 2016Article
- An Effective Deuterium Exchange Method for Neutron Crystal Structure Analysis with Unfolding-Refolding Processes.Molecular biotechnology · 2016Article
- Nuclear Magnetic Resonance Structure of a Novel Globular Domain in RBM10 Containing OCRE, the Octamer Repeat Sequence Motif.Structure (London, England : 1993) · 2016Article
- Cofactor-induced reversible folding of Flavodoxin-4 from Lactobacillus acidophilus.Protein science : a publication of the Protein Society · 2015Article
- Non-Uniform Sampling and J-UNIO Automation for Efficient Protein NMR Structure Determination.Chemistry (Weinheim an der Bergstrasse, Germany) · 2015Article
- APSY-NMR for protein backbone assignment in high-throughput structural biology.Journal of biomolecular NMR · 2015Article
- NMR structure determination of the protein NP_344798.1 as the first representative of Pfam PF06042.Journal of biomolecular NMR · 2015Article
- J-UNIO protocol used for NMR structure determination of the 206-residue protein NP_346487.1 from Streptococcus pneumoniae TIGR4.Journal of biomolecular NMR · 2015Article
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Authors and funding
5 authors at 3 institutions in 3 countries.
Funding
Abstract
NMR-Profiles are quantitative one-dimensional (1D) presentations of 2D [¹⁵N, ¹H]-correlation spectra used to monitor the quality of protein solutions prior to and during NMR structure determinations and functional studies. In our current use in structural genomics projects, an NMR-Profile is recorded at the outset of a structure determination, using a uniformly ¹⁵N-labeled microscale sample of the protein. We thus assess the extent to which polypeptide backbone resonance assignments can be achieved with given NMR techniques, for example, conventional triple resonance experiments or APSY-NMR. With the availability of sequence-specific polypeptide backbone resonance assignments in the course of the structure determination, an "Assigned NMR-Profile" is generated, which visualizes the variation of the ¹⁵N - ¹H correlation cross peak intensities along the sequence and thus maps the sequence locations of polypeptide segments for which the NMR line shapes are affected by conformational exchange or other processes. The Assigned NMR-Profile provides a guiding reference during later stages of the structure determination, and is of special interest for monitoring the protein during functional studies, where dynamic features may be modulated during physiological processes.
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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.