Pure shift amide detection in conventional and TROSY-type experiments of 13C,15N-labeled proteins

		BioNMR > Educational resources > Journal club
Pure shift amide detection in conventional and TROSY-type experiments of 13C,15N-labeled proteins

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:

Thread Tools

Search this Thread

Rate Thread

Display Modes

11-19-2022, 10:33 PM

nmrlearner

Senior Member

Join Date: Jan 2005

Posts: 23,808

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

Pure shift amide detection in conventional and TROSY-type experiments of 13C,15N-labeled proteins

Pure shift amide detection in conventional and TROSY-type experiments of 13C,15N-labeled proteins

Abstract

Large coupling networks in uniformly 13C,15N-labeled biomolecules induce broad multiplets that even in flexible proteins are frequently not recognized as such. The reason is that given multiplets typically consist of a large number of individual resonances that result in a single broad line, in which individual components are no longer resolved. We here introduce a real-time pure shift acquisition schemeÂ*for the detection of amide protons which is based on 13C-BIRDr,X. As a result the full homo- and heteronuclear coupling network can be suppressed at low power leading to real singlets at substantially improved resolution and uncompromised sensitivity. The method is tested on a small globular and an intrinsically disordered protein (IDP) where the average spectral resolution is increased by a factor ofâ??~â??2 and higher. Equally important, the approach works without saturation of water magnetization for solvent suppression and exchanging amide protons are not affected by saturation transfer.

Source: Journal of Biomolecular NMR

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
[NMR paper] Sensitivity-enhanced Four-dimensional Amide-amide Correlation NMR Experiments for Sequential Assignment of Proline-rich Disordered Proteins. Sensitivity-enhanced Four-dimensional Amide-amide Correlation NMR Experiments for Sequential Assignment of Proline-rich Disordered Proteins. Sensitivity-enhanced Four-dimensional Amide-amide Correlation NMR Experiments for Sequential Assignment of Proline-rich Disordered Proteins. J Am Chem Soc. 2018 Feb 28;: Authors: Wong LE, Maier J, Wienands J, Becker S, Griesinger C Abstract Proline is prevalent in intrinsically disordered proteins (IDPs). NMR assignment of proline-rich IDPs is a challenge due to low dispersion of chemical...	nmrlearner	Journal club	0	03-01-2018 09:20 PM
[NMR paper] Measurement of amide proton chemical shift anisotropy in perdeuterated proteins using CSA amplification Measurement of amide proton chemical shift anisotropy in perdeuterated proteins using CSA amplification Publication date: Available online 19 September 2017 Source:Journal of Magnetic Resonance</br> Author(s): Yuwei Ge, Ivan Hung, Xiaoli Liu, Maili Liu, Zhehong Gan, Conggang Li</br> Measuring 1H chemical shift anisotropy (CSA) is useful for probing proton environments and dynamics but remains a challenge due to strong homonuclear interaction and relatively small shift anisotropy, especially in proteins with multiple proton sites. Here the extended...	nmrlearner	Journal club	0	09-21-2017 02:38 AM
CH3] Labeled Proteins for Methyl-TROSY NMR - SelectScience CH3] Labeled Proteins for Methyl-TROSY NMR - SelectScience <img alt="" height="1" width="1"> CH3] Labeled Proteins for Methyl-TROSY NMR SelectScience Isotope labelling has revolutionized the use of biomolecular NMR spectroscopy, allowing the exploration of molecular interactions with high sensitivity and resolution. Introducing labelled Thr, a protein often found at molecular interfaces and involved ... Read here	nmrlearner	Online News	0	07-19-2017 01:32 PM
CH3] Labeled Proteins for Methyl-TROSY NMR - SelectScience CH3] Labeled Proteins for Methyl-TROSY NMR - SelectScience <img alt="" height="1" width="1"> CH3] Labeled Proteins for Methyl-TROSY NMR SelectScience Isotope labelling has revolutionized the use of biomolecular NMR spectroscopy, allowing the exploration of molecular interactions with high sensitivity and resolution. Introducing labelled Thr, a protein often found at molecular interfaces and involved ... and more » Read here	nmrlearner	Online News	0	07-17-2017 04:06 AM
CH3] Labeled Proteins for Methyl-TROSY NMR - SelectScience CH3] Labeled Proteins for Methyl-TROSY NMR - SelectScience <img alt="" height="1" width="1"> CH3] Labeled Proteins for Methyl-TROSY NMR SelectScience Isotope labelling has revolutionized the use of biomolecular NMR spectroscopy, allowing the exploration of molecular interactions with high sensitivity and resolution. Introducing labelled Thr, a protein often found at molecular interfaces and involved ... Read here	nmrlearner	Online News	0	07-14-2017 01:32 AM
Sequential backbone assignment based on dipolar amide-to-amide correlation experiments Sequential backbone assignment based on dipolar amide-to-amide correlation experiments Abstract Proton detection in solid-state NMR has seen a tremendous increase in popularity in the last years. New experimental techniques allow to exploit protons as an additional source of information on structure, dynamics, and protein interactions with their surroundings. In addition, sensitivity is mostly improved and ambiguity in assignment experiments reduced. We show here that, in the solid state, sequential amide-to-amide correlations turn out to be an...	nmrlearner	Journal club	0	05-15-2015 07:52 AM
Real-time pure shift 15 N HSQC of proteins: a real improvement in resolution and sensitivity Real-time pure shift 15 N HSQC of proteins: a real improvement in resolution and sensitivity Abstract Spectral resolution in proton NMR spectroscopy is reduced by the splitting of resonances into multiplets due to the effect of homonuclear scalar couplings. Although these effects are often hidden in protein NMR spectroscopy by low digital resolution and routine apodization, behind the scenes homonuclear scalar couplings increase spectral overcrowding. The possibilities for biomolecular NMR offered by new pure shift NMR methods are illustrated here....	nmrlearner	Journal club	0	03-04-2015 08:56 AM
[NMR paper] Suppression of diagonal peaks in TROSY-type 1H NMR NOESY spectra of 15N-labeled prote Suppression of diagonal peaks in TROSY-type 1H NMR NOESY spectra of 15N-labeled proteins. Related Articles Suppression of diagonal peaks in TROSY-type 1H NMR NOESY spectra of 15N-labeled proteins. J Magn Reson. 1999 Oct;140(2):499-503 Authors: Meissner A, Sørensen OW A novel method for suppression of diagonal peaks in the amide region of NOESY NMR spectra of 15N-labeled proteins is presented. The method is particularly useful for larger proteins at high magnetic fields where interference between dipolar and chemical shift anisotropy relaxation...	nmrlearner	Journal club	0	11-18-2010 08:31 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