NMR paper A (13)C-detected (15)N double-quantum NMR experiment to probe arginine side-chain guanidinium (15)N(?) chemical shifts.

		BioNMR > Educational resources > Journal club
[NMR paper] A (13)C-detected (15)N double-quantum NMR experiment to probe arginine side-chain guanidinium (15)N(?) chemical shifts.

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

11-13-2017, 12:45 AM

nmrlearner

Senior Member

Join Date: Jan 2005

Posts: 23,732

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

A (13)C-detected (15)N double-quantum NMR experiment to probe arginine side-chain guanidinium (15)N(?) chemical shifts.

A (13)C-detected (15)N double-quantum NMR experiment to probe arginine side-chain guanidinium (15)N(?) chemical shifts.

A (13)C-detected (15)N double-quantum NMR experiment to probe arginine side-chain guanidinium (15)N(?) chemical shifts.

J Biomol NMR. 2017 Nov 10;:

Authors: Mackenzie HW, Hansen DF

Abstract
Arginine side-chains are often key for enzyme catalysis, protein-ligand and protein-protein interactions. The importance of arginine stems from the ability of the terminal guanidinium group to form many key interactions, such as hydrogen bonds and salt bridges, as well as its perpetual positive charge. We present here an arginine (13)C(?)-detected NMR experiment in which a double-quantum coherence involving the two (15)N(?) nuclei is evolved during the indirect chemical shift evolution period. As the precession frequency of the double-quantum coherence is insensitive to exchange of the two (15)N(?); this new approach is shown to eliminate the previously deleterious line broadenings of (15)N(?) resonances caused by the partially restricted rotation about the C(?)-N(?) bond. Consequently, sharp and well-resolved (15)N(?) resonances can be observed. The utility of the presented method is demonstrated on the L99A mutant of the 19*kDa protein T4 lysozyme, where the measurement of small chemical shift perturbations, such as one-bond deuterium isotope shifts, of the arginine amine (15)N(?) nuclei becomes possible using the double-quantum experiment.

PMID: 29127559 [PubMed - as supplied by publisher]

More...

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
A 13 C-detected 15 N double-quantum NMR experiment to probe arginine side-chain guanidinium 15 N Î· chemical shifts A 13 C-detected 15 N double-quantum NMR experiment to probe arginine side-chain guanidinium 15 N Î· chemical shifts Abstract Arginine side-chains are often key for enzyme catalysis, proteinâ??ligand and proteinâ??protein interactions. The importance of arginine stems from the ability of the terminal guanidinium group to form many key interactions, such as hydrogen bonds and salt bridges, as well as its perpetual positive charge. We present here an arginine 13CÎ¶-detected NMR experiment in which a double-quantum coherence involving the two 15NÎ· nuclei...	nmrlearner	Journal club	0	11-10-2017 05:01 PM
Pressure dependence of side chain 13 C chemical shifts in model peptides Ac-Gly-Gly-Xxx-Ala-NH 2 Pressure dependence of side chain 13 C chemical shifts in model peptides Ac-Gly-Gly-Xxx-Ala-NH 2 Abstract For evaluating the pressure responses of folded as well as intrinsically unfolded proteins detectable by NMR spectroscopy the availability of data from well-defined model systems is indispensable. In this work we report the pressure dependence of 13C chemical shifts of the side chain atoms in the protected tetrapeptides Ac-Gly-Gly-Xxx-Ala-NH2 (Xxx, one of the 20 canonical amino acids). Contrary to expectation the chemical shifts of a number of...	nmrlearner	Journal club	0	09-14-2017 11:59 AM
[NMR paper] Determining rotational dynamics of the guanidino group of arginine side chains in proteins by carbon-detected NMR. Determining rotational dynamics of the guanidino group of arginine side chains in proteins by carbon-detected NMR. Related Articles Determining rotational dynamics of the guanidino group of arginine side chains in proteins by carbon-detected NMR. Chem Commun (Camb). 2017 Aug 25;: Authors: Gerecht K, Figueiredo AM, Hansen DF Abstract Arginine residues are imperative for many active sites and protein-interaction interfaces. A new NMR-based method is presented to determine the rotational dynamics around the N?-C? bond of...	nmrlearner	Journal club	0	08-26-2017 03:38 PM
[NMR paper] Probing arginine side-chains and their dynamics with carbon-detected NMR spectroscopy: application to the 42 kDa human histone deacetylase 8 at high pH. Probing arginine side-chains and their dynamics with carbon-detected NMR spectroscopy: application to the 42 kDa human histone deacetylase 8 at high pH. http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-2250-98-WileyOnlineLibrary-Button_120x27px_FullText.gif Related Articles Probing arginine side-chains and their dynamics with carbon-detected NMR spectroscopy: application to the 42 kDa human histone deacetylase 8 at high pH. Angew Chem Int Ed Engl. 2013 Mar 11;52(11):3145-7 Authors: Werbeck ND, Kirkpatrick J,...	nmrlearner	Journal club	0	01-29-2014 02:01 PM
A Simple Method to Measure Protein Side-Chain MobilityUsing NMR Chemical Shifts A Simple Method to Measure Protein Side-Chain MobilityUsing NMR Chemical Shifts Mark V. Berjanskii and David S. Wishart http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja407509z/aop/images/medium/ja-2013-07509z_0003.gif Journal of the American Chemical Society DOI: 10.1021/ja407509z http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA http://feeds.feedburner.com/~r/acs/jacsat/~4/qRQjRZhXxAM	nmrlearner	Journal club	0	09-23-2013 09:41 PM
[NMR paper] A simple method to measure protein side-chain mobility using NMR chemical shifts. A simple method to measure protein side-chain mobility using NMR chemical shifts. http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles A simple method to measure protein side-chain mobility using NMR chemical shifts. J Am Chem Soc. 2013 Sep 13; Authors: Berjanskii MV, Wishart DS Abstract Protein side-chain motions are involved in many important biological processes including enzymatic catalysis, allosteric regulation, and the mediation of protein-protein,...	nmrlearner	Journal club	0	09-17-2013 11:36 PM
[NMR paper] Assignment of the side-chain 1H and 13C resonances of interleukin-1 beta using double Assignment of the side-chain 1H and 13C resonances of interleukin-1 beta using double- and triple-resonance heteronuclear three-dimensional NMR spectroscopy. Related Articles Assignment of the side-chain 1H and 13C resonances of interleukin-1 beta using double- and triple-resonance heteronuclear three-dimensional NMR spectroscopy. Biochemistry. 1990 Sep 4;29(35):8172-84 Authors: Clore GM, Bax A, Driscoll PC, Wingfield PT, Gronenborn AM The assignment of the aliphatic 1H and 13C resonances of IL-1 beta, a protein of 153 residues and molecular...	nmrlearner	Journal club	0	08-21-2010 11:04 PM
arginine side chain assignment pulse wanted Hi, I want use 15N labeling for arginine side chain assignment. it seems the 2D HE(NE)HGHH is the right pulse to use ( J bio. NMR. 10(1997):193 ). You will be very appreciated for any information about getting this pulse. Thanks.	NMR_MSU_LU	NMR Questions and Answers	0	11-17-2006 09:39 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