NMR paper NMR Assignment of Methyl Groups in Immobilized Proteins Using Multiple-Bond 13C Homonuclear Transfers, Proton Detection, and Very Fast MAS

		BioNMR > Educational resources > Journal club
[NMR paper] NMR Assignment of Methyl Groups in Immobilized Proteins Using Multiple-Bond 13C Homonuclear Transfers, Proton Detection, and Very Fast MAS

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

04-15-2022, 03:24 PM

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

NMR Assignment of Methyl Groups in Immobilized Proteins Using Multiple-Bond 13C Homonuclear Transfers, Proton Detection, and Very Fast MAS

NMR Assignment of Methyl Groups in Immobilized Proteins Using Multiple-Bond 13C Homonuclear Transfers, Proton Detection, and Very Fast MAS

In nuclear magnetic resonance spectroscopy of proteins, methyl protons play a particular role as extremely sensitive reporters on dynamics, allosteric effects, and protein-protein interactions, accessible even in high-molecular-weight systems approaching 1 MDa. The notorious issue of their chemical shift assignment is addressed here by a joint use of solid-state ¹H-detected methods at very fast (nearly 100 kHz) magic-angle spinning, partial deuteration, and high-magnetic fields. The suitability...

More...

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
Complete assignment of Ala, Ile, Leu, Met and Val methyl groups of human blood group A and B glycosyltransferases using lanthanide-induced pseudocontact shifts and methylâ??methyl NOESY Complete assignment of Ala, Ile, Leu, Met and Val methyl groups of human blood group A and B glycosyltransferases using lanthanide-induced pseudocontact shifts and methylâ??methyl NOESY Abstract Human blood group A and B glycosyltransferases (GTA, GTB) are highly homologous glycosyltransferases. A number of high-resolution crystal structures is available showing that these enzymes convert from an open conformation into a catalytically active closed conformation upon substrate binding. However, the mechanism of glycosyltransfer is still under debate,...	nmrlearner	Journal club	0	04-26-2018 04:36 PM
[NMR paper] Proton-detected MAS NMR experiments based on dipolar transfers for backbone assignment of highly deuterated proteins. Proton-detected MAS NMR experiments based on dipolar transfers for backbone assignment of highly deuterated proteins. Related Articles Proton-detected MAS NMR experiments based on dipolar transfers for backbone assignment of highly deuterated proteins. J Magn Reson. 2014 Mar 4;242C:180-188 Authors: Chevelkov V, Habenstein B, Loquet A, Giller K, Becker S, Lange A Abstract Proton-detected solid-state NMR was applied to a highly deuterated insoluble, non-crystalline biological assembly, the Salmonella typhimurium type iii secretion system...	nmrlearner	Journal club	0	03-29-2014 01:00 PM
Proton-detected MAS NMR experiments based on dipolar transfers for backbone assignment of highly deuterated proteins Proton-detected MAS NMR experiments based on dipolar transfers for backbone assignment of highly deuterated proteins Publication date: Available online 4 March 2014 Source:Journal of Magnetic Resonance</br> Author(s): Veniamin Chevelkov , Birgit Habenstein , Antoine Loquet , Karin Giller , Stefan Becker , Adam Lange</br> Proton-detected solid-state NMR was applied to a highly deuterated insoluble, non-crystalline biological assembly, the Salmonella typhimurium type iii secretion system (T3SS) needle. Spectra of very high resolution and sensitivity were obtained...	nmrlearner	Journal club	0	03-04-2014 06:37 PM
[NMR paper] Specific labeling and assignment strategies of valine methyl groups for NMR studies of high molecular weight proteins. Specific labeling and assignment strategies of valine methyl groups for NMR studies of high molecular weight proteins. http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles Specific labeling and assignment strategies of valine methyl groups for NMR studies of high molecular weight proteins. J Biomol NMR. 2013 Sep 28; Authors: Mas G, Crublet E, Hamelin O, Gans P, Boisbouvier J Abstract The specific protonation of valine and leucine methyl...	nmrlearner	Journal club	0	10-01-2013 11:15 PM
[NMR paper] Out-and-back (13)C- (13)C scalar transfers in protein resonance assignment by proton-detected solid-state NMR under ultra-fast MAS. Out-and-back (13)C- (13)C scalar transfers in protein resonance assignment by proton-detected solid-state NMR under ultra-fast MAS. Related Articles Out-and-back (13)C- (13)C scalar transfers in protein resonance assignment by proton-detected solid-state NMR under ultra-fast MAS. J Biomol NMR. 2013 Jun 29; Authors: Barbet-Massin E, Pell AJ, Jaudzems K, Franks WT, Retel JS, Kotelovica S, Akopjana I, Tars K, Emsley L, Oschkinat H, Lesage A, Pintacuda G Abstract We present here (1)H-detected triple-resonance H/N/C experiments that...	nmrlearner	Journal club	0	07-03-2013 01:46 PM
Observation and Relaxation Properties of Individual Fast-Relaxing Proton Transitions in [CH3]-Methyl-Labeled, Deuterated Proteins Observation and Relaxation Properties of Individual Fast-Relaxing Proton Transitions in -Methyl-Labeled, Deuterated Proteins Publication year: 2012 Source: Journal of Magnetic Resonance, Available online 2 March 2012</br> HechaoSun, VitaliTugarinov</br> A pair of NMR experiments is developed for separation of individual fast-relaxing transitions inCH3methyl groups of methyl-protonated, highly deuterated proteins, and the measurement of their relaxation rates. Intra-methylH-H/H-C dipole-dipole cross-correlated spin relaxation that differentiates the rates of the fast-relaxing...	nmrlearner	Journal club	0	03-06-2012 06:04 AM
A simple biosynthetic method for stereospecific resonance assignment of prochiral methyl groups in proteins A simple biosynthetic method for stereospecific resonance assignment of prochiral methyl groups in proteins Abstract A new method for stereospecific assignment of prochiral methyl groups in proteins is presented in which protein samples are produced using U-glucose and subsaturating amounts of 2-methyl-acetolactate. The resulting non-uniform labeling pattern allows proR and proS methyl groups to be easily distinguished by their different phases in a constant-time two-dimensional 1H-13C correlation spectra. Protein samples are conveniently prepared using the same media composition as the...	nmrlearner	Journal club	0	02-06-2011 07:42 PM
[NMR paper] Cross-correlated relaxation enhanced 1H[bond]13C NMR spectroscopy of methyl groups in Cross-correlated relaxation enhanced 1H13C NMR spectroscopy of methyl groups in very high molecular weight proteins and protein complexes. Related Articles Cross-correlated relaxation enhanced 1H13C NMR spectroscopy of methyl groups in very high molecular weight proteins and protein complexes. J Am Chem Soc. 2003 Aug 27;125(34):10420-8 Authors: Tugarinov V, Hwang PM, Ollerenshaw JE, Kay LE A comparison of HSQC and HMQC pulse schemes for recording (1)H(13)C correlation maps of protonated methyl groups in highly deuterated proteins is presented....	nmrlearner	Journal club	0	11-24-2010 09:16 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