Anthranilic acid, the new player in the ensemble of aromatic residue labeling precursor compounds

		BioNMR > Educational resources > Journal club
Anthranilic acid, the new player in the ensemble of aromatic residue labeling precursor compounds

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

08-31-2017, 01:22 PM

nmrlearner

Senior Member

Join Date: Jan 2005

Posts: 23,733

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

Anthranilic acid, the new player in the ensemble of aromatic residue labeling precursor compounds

Anthranilic acid, the new player in the ensemble of aromatic residue labeling precursor compounds

Abstract

The application of metabolic precursors for selective stable isotope labeling of aromatic residues in cell-based protein overexpression has already resulted in numerous NMR probes to study the structural and dynamic characteristics of proteins. With anthranilic acid, we present the structurally simplest precursor for exclusive tryptophan side chain labeling. A synthetic route to 13C, 2H isotopologues allows the installation of isolated 13Câ??1H spin systems in the indole ring of tryptophan, representing a versatile tool to investigate side chain motion using relaxation-based experiments without the loss of magnetization due to strong 1JCC and weaker 2JCH scalar couplings, as well as dipolar interactions with remote hydrogens. In this article, we want to introduce this novel precursor in the context of hitherto existing techniques of in vivo aromatic residue labeling.

Source: Journal of Biomolecular NMR

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
Increased resolution of aromatic cross peaks using alternate 13 C labeling and TROSY Increased resolution of aromatic cross peaks using alternate 13 C labeling and TROSY Abstract For typical globular proteins, contacts involving aromatic side chains would constitute the largest number of distance constraints that could be used to define the structure of proteins and protein complexes based on NOE contacts. However, the 1H NMR signals of aromatic side chains are often heavily overlapped, which hampers extensive use of aromatic NOE cross peaks. Some of this overlap can be overcome by recording 13C-dispersed NOESY spectra. However, the...	nmrlearner	Journal club	0	05-10-2015 07:49 PM
[NMR images] 1D 1H, 2.0 mM, pH 7.4 spectrum for anthranilic acid, bmse000067 http://bmrb.protein.osaka-u.ac.jp/metabolomics/standards/anthranilic_acid/nmr/bmse000067/spectra_png/1H_2/00.png 7/06/2014 7:13:57 PM GMT 1D 1H, 2.0 mM, pH 7.4 spectrum for anthranilic acid, bmse000067 More...	nmrlearner	NMR pictures	0	06-07-2014 07:12 PM
[NMR paper] NMR analysis of cross strand aromatic interactions in an 8 residue hairpin and a 14 residue three stranded ?-sheet peptide. NMR analysis of cross strand aromatic interactions in an 8 residue hairpin and a 14 residue three stranded ?-sheet peptide. http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles NMR analysis of cross strand aromatic interactions in an 8 residue hairpin and a 14 residue three stranded ?-sheet peptide. J Phys Chem B. 2012 Dec 13;116(49):14207-15 Authors: Sonti R, Rai R, Ragothama S, Balaram P Abstract Cross strand aromatic interactions between a facing pair of...	nmrlearner	Journal club	0	06-13-2013 06:14 PM
[NMR paper] pH-Dependent Conformation, Dynamics, and Aromatic Interaction oftheGating Tryptophan Residue of the Influenza M2 Proton Channel fromSolid-State NMR. pH-Dependent Conformation, Dynamics, and Aromatic Interaction oftheGating Tryptophan Residue of the Influenza M2 Proton Channel fromSolid-State NMR. Related Articles pH-Dependent Conformation, Dynamics, and Aromatic Interaction oftheGating Tryptophan Residue of the Influenza M2 Proton Channel from*Solid-State NMR. Biophys J. 2013 Apr 16;104(8):1698-708 Authors: Williams JK, Zhang Y, Schmidt-Rohr K, Hong M Abstract The M2 protein of the influenza virus conducts protons into the virion under external acidic pH. The proton selectivity of...	nmrlearner	Journal club	0	04-23-2013 08:37 PM
High-Resolution Zero-Field NMR J-Spectroscopyof Aromatic Compounds High-Resolution Zero-Field NMR J-Spectroscopyof Aromatic Compounds John W. Blanchard, Micah P. Ledbetter, Thomas Theis, Mark C. Butler, Dmitry Budker and Alexander Pines http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja312239v/aop/images/medium/ja-2012-12239v_0005.gif Journal of the American Chemical Society DOI: 10.1021/ja312239v http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA http://feeds.feedburner.com/~r/acs/jacsat/~4/JnJRR_YbZhQ	nmrlearner	Journal club	0	02-27-2013 06:45 AM
Alternative SAIL-Trp for robust aromatic signal assignment and determination of the Ï?2 conformation by intra-residue NOEs Alternative SAIL-Trp for robust aromatic signal assignment and determination of the Ï?2 conformation by intra-residue NOEs Abstract Tryptophan (Trp) residues are frequently found in the hydrophobic cores of proteins, and therefore, their side-chain conformations, especially the precise locations of the bulky indole rings, are critical for determining structures by NMR. However, when analyzing -proteins, the observation and assignment of the ring signals are often hampered by excessive overlaps and tight spin couplings. These difficulties have been greatly alleviated by using...	nmrlearner	Journal club	0	09-27-2011 07:04 AM
Analysis of the amide 15N chemical shift tensor of the CÎ± tetrasubstituted constituent of membrane-active peptaibols, the Î±-aminoisobutyric acid residue, compared to those of di- and tri-substituted proteinogenic amino acid residues Analysis of the amide 15N chemical shift tensor of the CÎ± tetrasubstituted constituent of membrane-active peptaibols, the Î±-aminoisobutyric acid residue, compared to those of di- and tri-substituted proteinogenic amino acid residues <div class="Abstract">Abstract In protein NMR spectroscopy the chemical shift provides important information for the assignment of residues and a first structural evaluation of dihedral angles. Furthermore, angular restraints are obtained from oriented samples by solution and solid-state NMR spectroscopic approaches. Whereas the anisotropy of chemical...	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