Related ArticlesStudying intact bacterial peptidoglycan by proton-detected NMR spectroscopy at 100 kHz MAS frequency.
J Struct Biol. 2019 04 01;206(1):66-72
Authors: Bougault C, Ayala I, Vollmer W, Simorre JP, Schanda P
Abstract
The bacterial cell wall is composed of the peptidoglycan (PG), a large polymer that maintains the integrity of the bacterial cell. Due to its multi-gigadalton size, heterogeneity, and dynamics, atomic-resolution studies are inherently complex. Solid-state NMR is an important technique to gain insight into its structure, dynamics and interactions. Here, we explore the possibilities to study the PG with ultra-fast (100 kHz) magic-angle spinning NMR. We demonstrate that highly resolved spectra can be obtained, and show strategies to obtain site-specific resonance assignments and distance information. We also explore the use of proton-proton correlation experiments, thus opening the way for NMR studies of intact cell walls without the need for isotope labeling.
Dynamic domains of amyloid fibrils can be site-specifically assigned with proton detected 3D NMR spectroscopy
Dynamic domains of amyloid fibrils can be site-specifically assigned with proton detected 3D NMR spectroscopy
Abstract
Several amyloid fibrils have cores framed by highly dynamic, intrinsically disordered, domains that can play important roles for function and toxicity. To study these domains in detail using solid-state NMR spectroscopy, site-specific resonance assignments are required. Although the rapid dynamics of these domains lead to considerable averaging of orientation-dependent NMR interactions and thereby line-narrowing, the proton...
nmrlearner
Journal club
0
11-19-2016 08:35 PM
[NMR paper] Posttranslational Modifications of Intact Proteins Detected by NMR Spectroscopy: Application to Glycosylation.
Posttranslational Modifications of Intact Proteins Detected by NMR Spectroscopy: Application to Glycosylation.
Related Articles Posttranslational Modifications of Intact Proteins Detected by NMR Spectroscopy: Application to Glycosylation.
Angew Chem Int Ed Engl. 2015 Apr 29;
Authors: Schubert M, Walczak MJ, Aebi M, Wider G
Abstract
Posttranslational modifications (PTMs) are an integral part of the majority of proteins. The characterization of structure and function of PTMs can be very challenging especially for glycans. Existing...
nmrlearner
Journal club
0
05-01-2015 01:34 PM
[NMR paper] Proton-detected 2D radio frequency driven recoupling solid-state NMR studies on micelle-associated cytochrome-b5.
Proton-detected 2D radio frequency driven recoupling solid-state NMR studies on micelle-associated cytochrome-b5.
Related Articles Proton-detected 2D radio frequency driven recoupling solid-state NMR studies on micelle-associated cytochrome-b5.
J Magn Reson. 2014 Mar 1;242C:169-179
Authors: Pandey MK, Vivekanandan S, Yamamoto K, Im S, Waskell L, Ramamoorthy A
Abstract
Solid-state NMR spectroscopy is increasingly used in the high-resolution structural studies of membrane-associated proteins and peptides. Most such studies necessitate...
nmrlearner
Journal club
0
03-25-2014 11:49 AM
[NMR paper] Proton-Detected 2D Radio Frequency Driven Recoupling Solid-state NMR Studies on Micelle-associated Cytochrome-b5
Proton-Detected 2D Radio Frequency Driven Recoupling Solid-state NMR Studies on Micelle-associated Cytochrome-b5
Publication date: Available online 1 March 2014
Source:Journal of Magnetic Resonance</br>
Author(s): Manoj Kumar Pandey , Subramanian Vivekanandan , Kazutoshi Yamamoto , Sangchoul Im , Lucy Waskell , Ayyalusamy Ramamoorthy</br>
Solid-state NMR spectroscopy is increasingly used in the high-resolution structural studies of membrane-associated proteins and peptides. Most such studies necessitate isotopically labeled (13C, 15N and 2H) proteins/peptides,...
nmrlearner
Journal club
0
03-02-2014 01:53 AM
Solid-state NMR analysis of membrane proteins and protein aggregates by proton detected spectroscopy
Solid-state NMR analysis of membrane proteins and protein aggregates by proton detected spectroscopy
Abstract Solid-state NMR has emerged as an important tool for structural biology and chemistry, capable of solving atomic-resolution structures for proteins in membrane-bound and aggregated states. Proton detection methods have been recently realized under fast magic-angle spinning conditions, providing large sensitivity enhancements for efficient examination of uniformly labeled proteins. The first and often most challenging step of protein structure determination by NMR is the...
nmrlearner
Journal club
0
09-20-2012 06:06 AM
Rapid Measurement of PseudocontactShifts in Metalloproteinsby Proton-Detected Solid-State NMR Spectroscopy
Rapid Measurement of PseudocontactShifts in Metalloproteinsby Proton-Detected Solid-State NMR Spectroscopy
Michael J. Knight, Isabella C. Felli, Roberta Pierattelli, Ivano Bertini, Lyndon Emsley, Torsten Herrmann and Guido Pintacuda
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja306813j/aop/images/medium/ja-2012-06813j_0004.gif
Journal of the American Chemical Society
DOI: 10.1021/ja306813j
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/eCGR552L3hw
nmrlearner
Journal club
0
08-31-2012 09:37 PM
Proton-Detected Solid-State NMR Spectroscopy of Fibrillar and Membrane Proteins.
Proton-Detected Solid-State NMR Spectroscopy of Fibrillar and Membrane Proteins.
Proton-Detected Solid-State NMR Spectroscopy of Fibrillar and Membrane Proteins.
Angew Chem Int Ed Engl. 2011 Apr 20;
Authors: Linser R, Dasari M, Hiller M, Higman V, Fink U, Lopez Del Amo JM, Markovic S, Handel L, Kessler B, Schmieder P, Oesterhelt D, Oschkinat H, Reif B
nmrlearner
Journal club
0
04-22-2011 02:00 PM
Proton-Detected Solid-State NMR Spectroscopy of Fibrillar and Membrane Proteins.
Proton-Detected Solid-State NMR Spectroscopy of Fibrillar and Membrane Proteins.
Proton-Detected Solid-State NMR Spectroscopy of Fibrillar and Membrane Proteins.
Angew Chem Int Ed Engl. 2011 Apr 14;
Authors: Linser R, Dasari M, Hiller M, Higman V, Fink U, Lopez Del Amo JM, Markovic S, Handel L, Kessler B, Schmieder P, Oesterhelt D, Oschkinat H, Reif B