We present a multidimensional magic-angle spinning (MAS) solid-state NMR (ssNMR) study to characterize native Pseudomonas fluorescens colony biofilms at natural abundance without isotope-labelling. By using a high-resolution INEPT-based 2D ¹H-^(13)C ssNMR spectrum and thorough peak deconvolution at the 1D ssNMR spectra, approximately 80/134 (in 1D/2D) distinct biofilm chemical sites were identified. We compared CP and INEPT ^(13)C ssNMR spectra to differentiate signals originating from the...
[NMR paper] Tapping into the native Pseudomonas Bacterial Biofilm Structure by High-Resolution 1D and 2D MAS solid-state NMR
Tapping into the native Pseudomonas Bacterial Biofilm Structure by High-Resolution 1D and 2D MAS solid-state NMR
We present a high-resolution 1D and 2D magic-angle spinning (MAS) solid-state NMR (ssNMR) study to characterize native Pseudomonas fluorescens colony biofilms at natural abundance without isotope-labelling. By using a high-resolution INEPT-based 2D ¹ H- ^(13) C ssNMR spectrum and thorough peak deconvolution approach at the 1D ssNMR spectra, approximately 80/134 (in 1D/2D) distinct biofilm chemical sites were identified. We compared CP and INEPT ^(13) C ssNMR spectra to different...
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10-24-2023 07:00 PM
[NMR paper] Solution-state NMR assignment and secondary structure analysis of the monomeric Pseudomonas biofilm-forming functional amyloid accessory protein FapA
Solution-state NMR assignment and secondary structure analysis of the monomeric Pseudomonas biofilm-forming functional amyloid accessory protein FapA
FapA is an accessory protein within the biofilm forming functional bacterial amyloid related fap-operon in Pseudomonas, and maybe a chaperone for FapC controlling its fibrillization. To allow further structural analysis, here we present a complete sequential assignment of ¹H(amide), ^(13)C(?), ^(13)C(?), and ^(15)N NMR resonances for the functional form of the monomeric soluble FapA protein, comprising amino acids between 29 and 152. From...
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10-06-2023 10:37 PM
[NMR paper] Characterizing proteins in a native bacterial environment using solid-state NMR spectroscopy.
Characterizing proteins in a native bacterial environment using solid-state NMR spectroscopy.
Related Articles Characterizing proteins in a native bacterial environment using solid-state NMR spectroscopy.
Nat Protoc. 2021 Jan 13;:
Authors: Narasimhan S, Pinto C, Lucini Paioni A, van der Zwan J, Folkers GE, Baldus M
Abstract
For a long time, solid-state nuclear magnetic resonance (ssNMR) has been employed to study complex biomolecular systems at the detailed chemical, structural, or dynamic level. Recent progress in...
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01-15-2021 04:25 PM
[NMR paper] High-resolution NMR in the native state.
High-resolution NMR in the native state.
Related Articles High-resolution NMR in the native state.
IUCrJ. 2017 Mar 01;4(Pt 2):102-103
Authors: Baldus M
Abstract
High-resolution NMR provides increasing possibilities to probe biomolecular structure in the native state. In this issue, Luchinat and Banci discuss progress on using in-cell NMR in prokaryotic and eukaryotic cell preparations.
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03-03-2017 10:56 PM
Ultra-high resolution in MAS solid-state NMR of perdeuterated proteins: Implications for structure and dynamics
Ultra-high resolution in MAS solid-state NMR of perdeuterated proteins: Implications for structure and dynamics
Publication year: 2012
Source:Journal of Magnetic Resonance, Volume 216</br>
Bernd Reif</br>
High resolution proton spectra are obtained in MAS solid-state NMR in case samples are prepared using perdeuterated protein and D2O in the recrystallization buffer. Deuteration reduces drastically 1H, 1H dipolar interactions and allows to obtain amide proton line widths on the order of 20 Hz. Similarly, high-resolution proton spectra of aliphatic groups can be obtained...
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03-13-2012 03:33 PM
[NMR paper] Protein structure determination by high-resolution solid-state NMR spectroscopy: appl
Protein structure determination by high-resolution solid-state NMR spectroscopy: application to microcrystalline ubiquitin.
Related Articles Protein structure determination by high-resolution solid-state NMR spectroscopy: application to microcrystalline ubiquitin.
J Am Chem Soc. 2005 Jun 22;127(24):8618-26
Authors: Zech SG, Wand AJ, McDermott AE
High-resolution solid-state NMR spectroscopy has become a promising method for the determination of three-dimensional protein structures for systems which are difficult to crystallize or exhibit low...
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11-25-2010 08:21 PM
[NMR paper] Resolution enhancement in multidimensional solid-state NMR spectroscopy of proteins u
Resolution enhancement in multidimensional solid-state NMR spectroscopy of proteins using spin-state selection.
Related Articles Resolution enhancement in multidimensional solid-state NMR spectroscopy of proteins using spin-state selection.
J Am Chem Soc. 2003 Oct 1;125(39):11816-7
Authors: Duma L, Hediger S, Brutscher B, Böckmann A, Emsley L
We show that the resolution of homonuclear multidimensional solid-state NMR correlation experiments can be significantly improved using transition selection and spin-state-selective polarization transfer...
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11-24-2010 09:16 PM
[NMR paper] High-resolution structure of the oligomerization domain of p53 by multidimensional NM
High-resolution structure of the oligomerization domain of p53 by multidimensional NMR.
Related Articles High-resolution structure of the oligomerization domain of p53 by multidimensional NMR.
Science. 1994 Jul 15;265(5170):386-91
Authors: Clore GM, Omichinski JG, Sakaguchi K, Zambrano N, Sakamoto H, Appella E, Gronenborn AM
The three-dimensional structure of the oligomerization domain (residues 319 to 360) of the tumor suppressor p53 has been solved by multidimensional heteronuclear magnetic resonance (NMR) spectroscopy. The domain forms a...
Tapping into the native Pseudomonas bacterial biofilm structure by high-resolution multidimensional solid-state NMR
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