Spectral editing of alanine, serine, and threonine in uniformly labeled proteins based on frequency-selective homonuclear recoupling in solid-state NMR

		BioNMR > Educational resources > Journal club
Spectral editing of alanine, serine, and threonine in uniformly labeled proteins based on frequency-selective homonuclear recoupling in solid-state NMR

Webservers

NMR processing:

MDD

NMR assignment:

Backbone:

Side-chains:

NOEs:

Structure from NMR restraints:

Ab initio:

Fragment-based:

Rosetta-NMR (Robetta)

Template-based:

GeNMR

I-TASSER

Refinement:

Amber

Structure from chemical shifts:

Fragment-based:

Homology-based:

Torsion angles from chemical shifts:

Preditor

TALOS

Promega- Proline

Secondary structure from chemical shifts:

CSI (via RCI server)

TALOS

MICS caps, β-turns

d2D

PECAN

Flexibility from chemical shifts:

RCI

Interactions from chemical shifts:

HADDOCK

Chemical shifts re-referencing:

NMR model quality:

NOEs, other restraints:

Chemical shifts:

RDCs:

Pseudocontact shifts:

Protein geomtery:

SAVES2 or SAVES4

Quality Control Check

NMR spectrum prediction:

FANDAS

MestReS

V-NMR

Flexibility from structure:

Backbone S2

Methyl S2

B-factor

Molecular dynamics:

Gromacs

Amber

Antechamber

Chemical shifts prediction:

From structure:

Shiftx2

Sparta+

Camshift

CH3shift- Methyl

ArShift- Aromatic

ShiftS

Proshift

PPM

CheShift-2- Cα

From sequence:

Shifty

Camcoil

Poulsen_rc_CS

Disordered proteins:

MAXOCC

Format conversion & validation:

CCPN

From NMR-STAR 3.1

Validate NMR-STAR 3.1

NMR sample preparation:

Protein disorder:

DisMeta

Protein solubility:

Isotope labeling:

Solid-state NMR:

View First Unread

Thread Tools

Search this Thread

Rate Thread

Display Modes

04-23-2021, 07:01 AM

nmrlearner

Senior Member

Join Date: Jan 2005

Posts: 23,178

Points: 193,617, Level: 100

Level up: 0%, 0 Points needed

Activity: 50.7%

Last Achievements

Award-Showcase

NMR Credits: 0

NMR Points: 193,617

Downloads: 0

Uploads: 0

Spectral editing of alanine, serine, and threonine in uniformly labeled proteins based on frequency-selective homonuclear recoupling in solid-state NMR

Spectral editing of alanine, serine, and threonine in uniformly labeled proteins based on frequency-selective homonuclear recoupling in solid-state NMR

Abstract

Spectral editing is crucial to simplify the crowded solid-state NMR spectra of proteins. New techniques are introduced to edit 13C-13C correlations of uniformly labeled proteins under moderate magic-angle spinning (MAS), based on our recent frequency-selective homonuclear recoupling sequences [Zhang et al., J. Phys. Chem. Lett. 2020, 11, 8077â??8083]. The signals of alanine, serine, or threonine residues are selected out by selective 13CÎ±-13CÎ² double-quantum filtering (DQF). The 13CÎ±-13CÎ² correlations of alanine residues are selectively established with efficiency up toâ??~â??1.8 times that by dipolar-assisted rotational resonance (DARR). The techniques are shown in 2D/3D NCCX experiments and applied to the uniformly 13C, 15N labeled Aquaporin Z (AqpZ) membrane protein, demonstrating their potential to simplify spectral analyses in biological solid-state NMR.

Source: Journal of Biomolecular NMR

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
[NMR paper] Optimization of band-selective homonuclear dipolar recoupling in solid-state NMR by a numerical phase search. Optimization of band-selective homonuclear dipolar recoupling in solid-state NMR by a numerical phase search. Related Articles Optimization of band-selective homonuclear dipolar recoupling in solid-state NMR by a numerical phase search. J Chem Phys. 2019 Apr 21;150(15):154201 Authors: Zhang Z, Liu H, Deng J, Tycko R, Yang J Abstract Spin polarization transfers among aliphatic 13C nuclei, especially 13C?-13C? transfers, permit correlations of their nuclear magnetic resonance (NMR) frequencies that are essential for signal...	nmrlearner	Journal club	0	04-22-2019 06:11 PM
[NMR paper] Hidden motions and motion-induced invisibility: dynamics-based spectral editing in solid-state NMR. Hidden motions and motion-induced invisibility: dynamics-based spectral editing in solid-state NMR. Related Articles Hidden motions and motion-induced invisibility: dynamics-based spectral editing in solid-state NMR. Methods. 2018 Apr 24;: Authors: Matlahov I, van der Wel PCA Abstract Solid-state nuclear magnetic resonance (ssNMR) spectroscopy enables the structural characterization of a diverse array of biological assemblies that include amyloid fibrils, non-amyloid aggregates, membrane-associated proteins and viral capsids....	nmrlearner	Journal club	0	04-28-2018 03:16 PM
[NMR paper] Selective excitation for spectral editing and assignment in separated local field experiments of oriented membrane proteins Selective excitation for spectral editing and assignment in separated local field experiments of oriented membrane proteins Publication date: January 2017 Source:Journal of Magnetic Resonance, Volume 274</br> Author(s): Sophie N. Koroloff, Alexander A. Nevzorov</br> Spectroscopic assignment of NMR spectra for oriented uniformly labeled membrane proteins embedded in their native-like bilayer environment is essential for their structure determination. However, sequence-specific assignment in oriented-sample (OS) NMR is often complicated by insufficient resolution...	nmrlearner	Journal club	0	11-19-2016 08:35 PM
[NMR paper] Aromatic spectral editing techniques for magic-angle-spinning solid-state NMR spectroscopy of uniformly (13)C-labeled proteins. Aromatic spectral editing techniques for magic-angle-spinning solid-state NMR spectroscopy of uniformly (13)C-labeled proteins. Aromatic spectral editing techniques for magic-angle-spinning solid-state NMR spectroscopy of uniformly (13)C-labeled proteins. Solid State Nucl Magn Reson. 2015 Sep 14; Authors: Williams JK, Schmidt-Rohr K, Hong M Abstract The four aromatic amino acids in proteins, namely histidine, phenylalanine, tyrosine, and tryptophan, have strongly overlapping (13)C chemical shift ranges between 100 and 160ppm,...	nmrlearner	Journal club	0	10-07-2015 11:27 AM
Aromatic spectral editing Techniques for magic-Angle-spinning solid-state NMR spectroscopy of uniformly 13C-labeled proteins Aromatic spectral editing Techniques for magic-Angle-spinning solid-state NMR spectroscopy of uniformly 13C-labeled proteins Publication date: Available online 14 September 2015 Source:Solid State Nuclear Magnetic Resonance</br> Author(s): Jonathan K. Williams, Klaus Schmidt-Rohr, Mei Hong</br> The four aromatic amino acids in proteins, namely histidine, phenylalanine, tyrosine, and tryptophan, give highly overlapped 13C chemical shifts between 100 and 160ppm, and have so far been largely neglected in solid-state NMR determination of protein structures. Yet...	nmrlearner	Journal club	0	09-14-2015 10:42 PM
Restraints on backbone conformations in solid state NMR studies of uniformly labeled proteins from quantitative amide 15N–15N and carbonyl 13C–13C dipolar recoupling data Restraints on backbone conformations in solid state NMR studies of uniformly labeled proteins from quantitative amide 15N–15N and carbonyl 13C–13C dipolar recoupling data May 2012 Publication year: 2012 Source:Journal of Magnetic Resonance, Volume 218</br> </br> Recent structural studies of uniformly 15N, 13C-labeled proteins by solid state nuclear magnetic resonance (NMR) rely principally on two sources of structural restraints: (i) restraints on backbone conformation from isotropic 15N and 13C chemical shifts, based on empirical correlations between chemical shifts and...	nmrlearner	Journal club	0	02-03-2013 10:13 AM
Restraints on backbone conformations in solid state NMR studies of uniformly labeled proteins from quantitative amide 15N-15N and carbonyl 13C-13C dipolar recoupling data Restraints on backbone conformations in solid state NMR studies of uniformly labeled proteins from quantitative amide 15N-15N and carbonyl 13C-13C dipolar recoupling data Publication year: 2012 Source:Journal of Magnetic Resonance</br> Kan-Nian Hu, Wei Qiang, Guillermo A. Bermejo, Charles D. Schwieters, Robert Tycko</br> Recent structural studies of uniformly 15N,13C-labeled proteins by solid state nuclear magnetic resonance (NMR) rely principally on two sources of structural restraints: (i) restraints on backbone conformation from isotropic 15N and 13C chemical...	nmrlearner	Journal club	0	03-10-2012 10:54 AM
Radio frequency assisted homonuclear recoupling - A Floquet description of homonuclear recoupling via surrounding heteronuclei in fully protonated to fully deuterated systems Radio frequency assisted homonuclear recoupling - A Floquet description of homonuclear recoupling via surrounding heteronuclei in fully protonated to fully deuterated systems Publication year: 2011 Source: Journal of Magnetic Resonance, In Press, Accepted Manuscript, Available online 18 January 2011</br> Michal, Leskes , Ümit, Akbey , Hartmut, Oschkinat , Barth-Jan, van Rossum , Shimon, Vega</br> We present a Floquet theory approach for the analysis of homonuclear recoupling assisted by radio frequency (RF) irradiation of surrounding heteronuclear spins. This description covers a...	nmrlearner	Journal club	0	01-19-2011 03:04 PM

« Previous Thread | Next Thread »

Posting Rules
You may not post new threads You may not post replies You may not post attachments You may not edit your posts BB code is On Smilies are On [IMG] code is On HTML code is On Trackbacks are Off Pingbacks are Off Refbacks are Off