Abstract
Biomolecular solid-state NMR experiments have traditionally been collected through detection of (13)C or (15)N nuclei. Since these nuclei have relatively low sensitivity stemming from their smaller gyromagnetic ratios relative to (1)H, the time required to collect multi-dimensional datasets serves as a limitation to resonance assignment and structure determination. One improvement in the field has been to employ simultaneous or parallel acquisition techniques with the goal of acquiring more than one dataset at a time and therefore speeding up the overall data collection process. Central to these experiments is the cross-polarization (CP) element, which serves as a way to transfer magnetization between nuclei via magnetic dipolar couplings. In this chapter, we show how residual signal remaining after CP is a polarization source that can be used to acquire additional datasets. The setup of this class of experiments, referred to as Afterglow spectroscopy, is described and demonstrated using a membrane protein transporter involved in multidrug resistance.
[NMR paper] Proton-Detected NMR Spectroscopy of Nanodisc-Embedded Membrane Proteins: MAS Solid-State vs. Solution-State Methods.
Proton-Detected NMR Spectroscopy of Nanodisc-Embedded Membrane Proteins: MAS Solid-State vs. Solution-State Methods.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Proton-Detected NMR Spectroscopy of Nanodisc-Embedded Membrane Proteins: MAS Solid-State vs. Solution-State Methods.
J Phys Chem B. 2017 Jul 24;:
Authors: Lakomek NA, Frey L, Bibow S, Böckmann A, Riek R, Meier BH
Abstract
The structural and dynamical characterization of membrane proteins...
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07-25-2017 07:46 PM
[NMR paper] Investigation of rhodopsin dynamics in its signaling state by solid-state deuterium NMR spectroscopy.
Investigation of rhodopsin dynamics in its signaling state by solid-state deuterium NMR spectroscopy.
Investigation of rhodopsin dynamics in its signaling state by solid-state deuterium NMR spectroscopy.
Methods Mol Biol. 2015;1271:133-58
Authors: Struts AV, Chawla U, Perera SM, Brown MF
Abstract
Site-directed deuterium NMR spectroscopy is a valuable tool to study the structural dynamics of biomolecules in cases where solution NMR is inapplicable. Solid-state (2)H NMR spectral studies of aligned membrane samples of rhodopsin...
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[NMR paper] Solid-state NMR spectroscopy of the HIV gp41 membrane fusion protein supports intermolecular antiparallel ? sheet fusion peptide structure in the final six-helix bundle state.
Solid-state NMR spectroscopy of the HIV gp41 membrane fusion protein supports intermolecular antiparallel ? sheet fusion peptide structure in the final six-helix bundle state.
Related Articles Solid-state NMR spectroscopy of the HIV gp41 membrane fusion protein supports intermolecular antiparallel ? sheet fusion peptide structure in the final six-helix bundle state.
J Mol Biol. 2013 Nov 15;
Authors: Sackett K, Nethercott MJ, Zheng Z, Weliky DP
Abstract
The HIV gp41 protein catalyzes fusion between viral and target cell membranes. Although...
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Solid-state NMR spectroscopy of the HIV gp41 membrane fusion protein supports intermolecular antiparallel ? sheet fusion peptide structure in the final six-helix bundle state
Solid-state NMR spectroscopy of the HIV gp41 membrane fusion protein supports intermolecular antiparallel ? sheet fusion peptide structure in the final six-helix bundle state
Publication date: Available online 16 November 2013
Source:Journal of Molecular Biology</br>
Author(s): Kelly Sackett , Matthew J. Nethercott , Zhaoxiong Zheng , David P. Weliky</br>
The HIV gp41 protein catalyzes fusion between viral and target cell membranes. Although the ~20-residue N-terminal fusion peptide (FP) region is critical for fusion, the structure of this region is not...
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Solid-State NMR Spectroscopy of Proteins
From The DNP-NMR Blog:
Solid-State NMR Spectroscopy of Proteins
A nice review about solid-state NMR spectroscopy with some solid-state DNP.
Müller, H., M. Etzkorn, and H. Heise, Solid-State NMR Spectroscopy of Proteins, in Modern NMR Methodology, H. Heise and S. Matthews, Editors. 2013, Springer Berlin Heidelberg. p. 121-156.
Detecting the "Afterglow" of (13)C NMR in Proteins Using Multiple Receivers.
Detecting the "Afterglow" of (13)C NMR in Proteins Using Multiple Receivers.
Related Articles Detecting the "Afterglow" of (13)C NMR in Proteins Using Multiple Receivers.
J Am Chem Soc. 2010 Dec 2;
Authors: Kupc?e E, Kay LE, Freeman R
We show that the weak signal that remains after (13)C-detected experiments (the (13)C "afterglow") can still be measured with high sensitivity by proton detection. This is illustrated by the incorporation of two experiments, 2D (HA)CACO and 3D (HA)CA(CO)NNH, into a single pulse sequence that makes use of two receivers...
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12-04-2010 07:24 PM
Detecting the “Afterglow” of 13C NMR in Proteins Using Multiple Receivers
Detecting the “Afterglow” of 13C NMR in Proteins Using Multiple Receivers
E?riks Kupc?e, Lewis E. Kay and Ray Freeman
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja1080025/aop/images/medium/ja-2010-080025_0002.gif
Journal of the American Chemical Society
DOI: 10.1021/ja1080025
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/YNH74d-9ntc
Afterglow Solid-State NMR Spectroscopy.
Linear Mode
