Side-chain to backbone correlations from solid-state NMR of perdeuterated proteins through combined excitation and long-range magnetization transfers.

		BioNMR > Educational resources > Journal club
Side-chain to backbone correlations from solid-state NMR of perdeuterated proteins through combined excitation and long-range magnetization transfers.

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

08-09-2011, 12:11 PM

nmrlearner

Senior Member

Join Date: Jan 2005

Posts: 23,777

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

Side-chain to backbone correlations from solid-state NMR of perdeuterated proteins through combined excitation and long-range magnetization transfers.

Side-chain to backbone correlations from solid-state NMR of perdeuterated proteins through combined excitation and long-range magnetization transfers.

Side-chain to backbone correlations from solid-state NMR of perdeuterated proteins through combined excitation and long-range magnetization transfers.

J Biomol NMR. 2011 Aug 7;

Authors: Linser R

Proteins with excessive deuteration give access to proton detected solid-state NMR spectra of extraordinary resolution and sensitivity. The high spectral quality achieved after partial proton back-exchange has been shown to start a new era for backbone assignment, protein structure elucidation, characterization of protein dynamics, and access to protein parts undergoing motion. The large absence of protons at non-exchangeable sites, however, poses a serious hurdle for characterization of side chains, which play an important role especially for structural understanding of the protein core and the investigation of protein-protein and protein-ligand interactions, e.g. This has caused the perdeuteration approach to almost exclusively be amenable to backbone characterization only. In this work it is shown that a combination of isotropic (13)C mixing with long-range (1)H/(13)C magnetization transfers can be used effectively to also access complete sets of side-chain chemical shifts in perdeuterated proteins and correlate these with the protein backbone with high unambiguity and resolution. COmbined POlarization from long-Range transfers And Direct Excitation (COPORADE) allows this strategy to yield complete sets of aliphatic amino acid resonances with reasonable sensitivity.

PMID: 21822966 [PubMed - as supplied by publisher]

Source: PubMed

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
Estimating side-chain order in methyl-protonated, perdeuterated proteins via multiple-quantum relaxation violated coherence transfer NMR spectroscopy Estimating side-chain order in methyl-protonated, perdeuterated proteins via multiple-quantum relaxation violated coherence transfer NMR spectroscopy Abstract Relaxation violated coherence transfer NMR spectroscopy (Tugarinov et al. in J Am Chem Soc 129:1743â??1750, 2007) is an established experimental tool for quantitative estimation of the amplitudes of side-chain motions in methyl-protonated, highly deuterated proteins. Relaxation violated coherence transfer experiments monitor the build-up of methyl proton multiple-quantum coherences that can be created in magnetically equivalent...	nmrlearner	Journal club	0	02-11-2012 10:31 AM
Ultra-high resolution in MAS solid-state NMR of perdeuterated proteins: Implications for Structure and Dynamics Ultra-high resolution in MAS solid-state NMR of perdeuterated proteins: Implications for Structure and Dynamics Publication year: 2012 Source: Journal of Magnetic Resonance, Available online 5 January 2012</br> Bernd*Reif</br> http://www.sciencedirect.com/cache/MiamiImageURL/1-s2.0-S1090780711005969-fx1.sml</br></br></br> Source: Journal of Magnetic Resonance	nmrlearner	Journal club	0	01-07-2012 03:12 PM
Backbone assignment of perdeuterated proteins using long-range H/C-dipolar transfers Backbone assignment of perdeuterated proteins using long-range H/C-dipolar transfers Abstract For micro-crystalline proteins, solid-state nuclear magnetic resonance spectroscopy of perdeuterated samples can provide spectra of unprecedented quality. Apart from allowing to detect sparsely introduced protons and thereby increasing the effective resolution for a series of sophisticated techniques, deuteration can provide extraordinary coherence lifetimesâ??obtainable for all involved nuclei virtually without decoupling and enabling the use of scalar magnetization transfers. Unfortunately,...	nmrlearner	Journal club	0	12-17-2011 04:44 AM
‘q-titration’ of long-chain and short-chain lipids differentiates between structured and mobile residues of membrane proteins studied in bicelles by solution NMR spectroscopy ‘q-titration’ of long-chain and short-chain lipids differentiates between structured and mobile residues of membrane proteins studied in bicelles by solution NMR spectroscopy Publication year: 2011 Source: Journal of Magnetic Resonance, Available online 25 October 2011</br> Woo SungSon, Sang HoPark, Henry J.Nothnagel, George J.Lu, Yan*Wang, ...</br> ‘q-titration’ refers to the systematic comparison of signal intensities in solution NMR spectra of uniformlyN labeled membrane proteins solubilized in micelles and isotropic bicelles as a function of the molar ratios (q) of the...	nmrlearner	Journal club	0	10-26-2011 11:25 AM
Side-chain to backbone correlations from solid-state NMR of perdeuterated proteins through combined excitation and long-range magnetization transfers Side-chain to backbone correlations from solid-state NMR of perdeuterated proteins through combined excitation and long-range magnetization transfers Abstract Proteins with excessive deuteration give access to proton detected solid-state NMR spectra of extraordinary resolution and sensitivity. The high spectral quality achieved after partial proton back-exchange has been shown to start a new era for backbone assignment, protein structure elucidation, characterization of protein dynamics, and access to protein parts undergoing motion. The large absence of protons at non-exchangeable...	nmrlearner	Journal club	0	08-11-2011 02:24 AM
Structure Calculation from Unambiguous Long-Range Amide and Methyl (1)H-(1)H Distance Restraints for a Microcrystalline Protein with MAS Solid-State NMR Spectroscopy. Structure Calculation from Unambiguous Long-Range Amide and Methyl (1)H-(1)H Distance Restraints for a Microcrystalline Protein with MAS Solid-State NMR Spectroscopy. Structure Calculation from Unambiguous Long-Range Amide and Methyl (1)H-(1)H Distance Restraints for a Microcrystalline Protein with MAS Solid-State NMR Spectroscopy. J Am Chem Soc. 2011 Mar 24; Authors: Linser R, Bardiaux B, Higman V, Fink U, Reif B Magic-angle spinning (MAS) solid-state NMR becomes an increasingly important tool for the determination of structures of membrane...	nmrlearner	Journal club	0	03-26-2011 07:00 PM
Structure Calculation from Unambiguous Long-Range Amide and Methyl 1H-1H Distance Restraints for a Microcrystalline Protein with MAS Solid-State NMR Spectroscopy Structure Calculation from Unambiguous Long-Range Amide and Methyl 1H-1H Distance Restraints for a Microcrystalline Protein with MAS Solid-State NMR Spectroscopy Rasmus Linser, Benjamin Bardiaux, Victoria Higman, Uwe Fink and Bernd Reif http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja110222h/aop/images/medium/ja-2010-10222h_0004.gif Journal of the American Chemical Society DOI: 10.1021/ja110222h http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA http://feeds.feedburner.com/~r/acs/jacsat/~4/Dh0EBf8PwcY	nmrlearner	Journal club	0	03-24-2011 08:02 PM
Optimum levels of exchangeable protons in perdeuterated proteins for proton detection in MAS solid-state NMR spectroscopy Optimum levels of exchangeable protons in perdeuterated proteins for proton detection in MAS solid-state NMR spectroscopy Abstract We present a systematic study of the effect of the level of exchangeable protons on the observed amide proton linewidth obtained in perdeuterated proteins. Decreasing the amount of D2O employed in the crystallization buffer from 90 to 0%, we observe a fourfold increase in linewidth for both 1H and 15N resonances. At the same time, we find a gradual increase in the signal-to-noise ratio (SNR) for 1Hâ??15N correlations in dipolar coupling based experiments for...	nmrlearner	Journal club	0	01-09-2011 12:46 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