Question from NMRWiki Q&A forum unusual tyrosine cross peaks

		BioNMR > NMR community > News from other NMR forums
[Question from NMRWiki Q&A forum] unusual tyrosine cross peaks

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

10-17-2011, 08:40 AM

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

unusual tyrosine cross peaks

unusual tyrosine cross peaks

Hi I am observing some unexpected cross peaks in some homonuclear protein data and I was wanting to know if anyone had an ideas what im looking at. I am looking at what I was confident was a tyrosine HE-HD cross peak in a TOCSY giving charachterticaly intense cross peaks at 6.9 x 6.4 ppm, however I then noticed a second set of TOCSY peaks to both the HE* and HD* at 5.4 ppm which also gives a COSY to the HE. These peaks shift together if I change the temperature sugesting it is not just two overlaped resonances, are still present in D2O, both the HE and HD* give the anticipated intensity in the 1D sugesting theses are not chemical exchange cross peaks. my initial gues was observation og the Tyr OH but the chemical shift doesnt really make sense and one wouldnt expect to see a COSY to the OH either, this is not ovrlaped with an NH2 or NH (by compsrison with my HSQC) any ideas, im at a bit of a loss and not sure if im just not missing an obvious explanation.Any help would be apreciatedTom

Check if somebody has answered this question on NMRWiki QA forum

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
[NMR paper] Unusual 1H NMR chemical shifts support (His) C(epsilon) 1...O==C H-bond: proposal for Unusual 1H NMR chemical shifts support (His) C(epsilon) 1...O==C H-bond: proposal for reaction-driven ring flip mechanism in serine protease catalysis. Related Articles Unusual 1H NMR chemical shifts support (His) C(epsilon) 1...O==C H-bond: proposal for reaction-driven ring flip mechanism in serine protease catalysis. Proc Natl Acad Sci U S A. 2000 Sep 12;97(19):10371-6 Authors: Ash EL, Sudmeier JL, Day RM, Vincent M, Torchilin EV, Haddad KC, Bradshaw EM, Sanford DG, Bachovchin WW 13C-selective NMR, combined with inhibitor perturbation...	nmrlearner	Journal club	0	11-19-2010 08:29 PM
[NMR paper] NMR solution structure of AlcR (1-60) provides insight in the unusual DNA binding pro NMR solution structure of AlcR (1-60) provides insight in the unusual DNA binding properties of this zinc binuclear cluster protein. Related Articles NMR solution structure of AlcR (1-60) provides insight in the unusual DNA binding properties of this zinc binuclear cluster protein. J Mol Biol. 2000 Jan 28;295(4):729-36 Authors: Cerdan R, Cahuzac B, Félenbok B, Guittet E The three-dimensional structure of the DNA-binding domain (residues 1-60) of the ethanol regulon transcription factor AlcR from Aspergillus nidulans has been solved by NMR....	nmrlearner	Journal club	0	11-18-2010 09:15 PM
[NMR paper] Tubulin-tyrosine ligase catalyzes covalent binding of 3-fluoro-tyrosine to tubulin: k Tubulin-tyrosine ligase catalyzes covalent binding of 3-fluoro-tyrosine to tubulin: kinetic and NMR studies. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Tubulin-tyrosine ligase catalyzes covalent binding of 3-fluoro-tyrosine to tubulin: kinetic and NMR studies. FEBS Lett. 1995 Oct 30;374(2):165-8 Authors: Monasterio O, Nova E, LÃ³pez-Brauet A, Lagos R The use of 3-fluoro-tyrosine as an alternative substrate for the enzyme tubulin:tyrosine ligase which catalyzes the...	nmrlearner	Journal club	0	08-22-2010 03:50 AM
[NMR paper] Unusual helix-containing greek keys in development-specific Ca(2+)-binding protein S. Unusual helix-containing greek keys in development-specific Ca(2+)-binding protein S. 1H, 15N, and 13C assignments and secondary structure determined with the use of multidimensional double and triple resonance heteronuclear NMR spectroscopy. Related Articles Unusual helix-containing greek keys in development-specific Ca(2+)-binding protein S. 1H, 15N, and 13C assignments and secondary structure determined with the use of multidimensional double and triple resonance heteronuclear NMR spectroscopy. Biochemistry. 1994 Mar 8;33(9):2409-21 Authors: Bagby S,...	nmrlearner	Journal club	0	08-22-2010 03:33 AM
[NMR paper] NMR analysis of the residual structure in the denatured state of an unusual mutant of NMR analysis of the residual structure in the denatured state of an unusual mutant of staphylococcal nuclease. Related Articles NMR analysis of the residual structure in the denatured state of an unusual mutant of staphylococcal nuclease. Structure. 1993 Oct 15;1(2):121-34 Authors: Shortle D, Abeygunawardana C BACKGROUND: Staphylococcal nuclease is a well-developed model system for analyzing the effects of mutations on protein folding and stability. Substitution of glycine 88 with valine (Gly88Val) destabilizes staphylococcal nuclease by 1.0...	nmrlearner	Journal club	0	08-22-2010 03:01 AM
[NMR paper] An unusual peptide conformation may precipitate amyloid formation in Alzheimer's dise An unusual peptide conformation may precipitate amyloid formation in Alzheimer's disease: application of solid-state NMR to the determination of protein secondary structure. Related Articles An unusual peptide conformation may precipitate amyloid formation in Alzheimer's disease: application of solid-state NMR to the determination of protein secondary structure. Biochemistry. 1991 Oct 29;30(43):10382-7 Authors: Spencer RG, Halverson KJ, Auger M, McDermott AE, Griffin RG, Lansbury PT The formation of insoluble proteinaceous deposits is...	nmrlearner	Journal club	0	08-21-2010 11:12 PM
[NMR paper] An unusual peptide conformation may precipitate amyloid formation in Alzheimer's dise An unusual peptide conformation may precipitate amyloid formation in Alzheimer's disease: application of solid-state NMR to the determination of protein secondary structure. Related Articles An unusual peptide conformation may precipitate amyloid formation in Alzheimer's disease: application of solid-state NMR to the determination of protein secondary structure. Biochemistry. 1991 Oct 29;30(43):10382-7 Authors: Spencer RG, Halverson KJ, Auger M, McDermott AE, Griffin RG, Lansbury PT The formation of insoluble proteinaceous deposits is...	nmrlearner	Journal club	0	08-21-2010 11:12 PM
[NMR paper] Unusual NMR, EPR, and MÃ¶ssbauer properties of Chromatium vinosum 2[4Fe-4S] ferredoxi Unusual NMR, EPR, and MÃ¶ssbauer properties of Chromatium vinosum 2 ferredoxin. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Unusual NMR, EPR, and MÃ¶ssbauer properties of Chromatium vinosum 2 ferredoxin. Biochemistry. 1999 May 11;38(19):6335-45 Authors: Kyritsis P, KÃ¼mmerle R, Huber JG, Gaillard J, Guigliarelli B, Popescu C, MÃ¼nck E, Moulis JM The ferredoxin from Chromatium vinosum (CvFd) exhibits sequence and structure peculiarities. Its two Fe4S4(SCys)4 clusters have unusually...	nmrlearner	Journal club	0	08-21-2010 04:03 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