NMR paper Four-dimensional heteronuclear triple-resonance NMR spectroscopy of interleukin-1 bet

		BioNMR > Educational resources > Journal club
[NMR paper] Four-dimensional heteronuclear triple-resonance NMR spectroscopy of interleukin-1 bet

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

08-21-2010, 11:04 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

Four-dimensional heteronuclear triple-resonance NMR spectroscopy of interleukin-1 bet

Four-dimensional heteronuclear triple-resonance NMR spectroscopy of interleukin-1 beta in solution.

Related Articles Four-dimensional heteronuclear triple-resonance NMR spectroscopy of interleukin-1 beta in solution.

Science. 1990 Jul 27;249(4967):411-4

Authors: Kay LE, Clore GM, Bax A, Gronenborn AM

A method is presented that dramatically improves the resolution of protein nuclear magnetic resonance (NMR) spectra by increasing their dimensionality to four. The power of this technique is demonstrated by the application of four-dimensional carbon-13--nitrogen-15 (13C-15N)--edited nuclear Overhauser effect (NOE) spectroscopy to interleukin-1 beta, a protein of 153 residues. The NOEs between NH and aliphatic protons are first spread out into a third dimension by the 15N chemical shift of the amide 15N atom and subsequently into a fourth dimension by the 13C chemical shift of the directly bonded 13C atoms. By this means ambiguities in the assignment of NOEs between NH and aliphatic protons that are still present in the three-dimensional 15N-edited NOE spectrum due to extensive chemical shift overlap and degeneracy of aliphatic resonances are completely removed. Consequently, many more approximate interproton distance restraints can be obtained from the NOE data than was heretofore possible, thereby expanding the horizons of three-dimensional structure determination by NMR to larger proteins.

PMID: 2377896 [PubMed - indexed for MEDLINE]

Source: PubMed

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
Three-dimensional triple-resonance NMR Spectroscopy of isotopically enriched proteins Three-dimensional triple-resonance NMR Spectroscopy of isotopically enriched proteins Publication year: 2011 Source: Journal of Magnetic Resonance, Volume 213, Issue 2, December 2011, Pages 423-441</br> Lewis E.Kay, MitsuhikoIkura, RolfTschudin, AdBax</br> Four new and complementary three-dimensional triple-resonance experiments are described for obtaining complete backboneH,C, andN resonance assignments of proteins uniformly enriched withC andN. The new methods all rely onH detection and use multiple magnetization transfers through well-resolved one-bondJcouplings. Therefore, the...	nmrlearner	Journal club	0	12-11-2011 07:57 AM
Triple resonance three-dimensional protein NMR: Before it became a black box. Triple resonance three-dimensional protein NMR: Before it became a black box. Triple resonance three-dimensional protein NMR: Before it became a black box. J Magn Reson. 2011 Aug 30; Authors: Bax A Abstract Three-dimensional triple resonance experiments have become an integral part of virtually every solution NMR study of proteins. The approach relies on uniform isotopic enrichment of proteins with (13)C and (15)N, and establishes the scalar connectivity pathway between nuclei through the large (1)J(NH), (1)J(CH)(, 1)J(CC), and (1)J(CN)...	nmrlearner	Journal club	0	09-03-2011 06:55 PM
Triple resonance three-dimensional protein NMR: Before it became a black box Triple resonance three-dimensional protein NMR: Before it became a black box Publication year: 2011 Source: Journal of Magnetic Resonance, In Press, Corrected Proof, Available online 31 August 2011</br> Ad, Bax</br> Three-dimensional triple resonance experiments have become an integral part of virtually every solution NMR study of proteins. The approach relies on uniform isotopic enrichment of proteins with 13C and 15N, and establishes the scalar connectivity pathway between nuclei through the large 1JNH, 1JCH, 1JCC, and 1JCN couplings. The magnetization transfer process takes place...	nmrlearner	Journal club	0	08-31-2011 07:12 PM
[NMR paper] Direct determination of the interleukin-6 binding epitope of the interleukin-6 recept Direct determination of the interleukin-6 binding epitope of the interleukin-6 receptor by NMR spectroscopy. Related Articles Direct determination of the interleukin-6 binding epitope of the interleukin-6 receptor by NMR spectroscopy. J Biol Chem. 2004 Jan 2;279(1):571-6 Authors: Schwantner A, Dingley AJ, Ozbek S, Rose-John S, Grötzinger J All cytokines belonging to the interleukin-6 (IL-6)-type family of cytokines utilize receptors that have a modular build of several immunoglobulin-like and fibronectin type III-like domains. Characteristic...	nmrlearner	Journal club	0	11-24-2010 09:16 PM
[NMR paper] Heteronuclear three-dimensional NMR spectroscopy of a partially denatured protein: th Heteronuclear three-dimensional NMR spectroscopy of a partially denatured protein: the A-state of human ubiquitin. Related Articles Heteronuclear three-dimensional NMR spectroscopy of a partially denatured protein: the A-state of human ubiquitin. J Biomol NMR. 1993 May;3(3):285-96 Authors: Stockman BJ, Euvrard A, Scahill TA Human ubiquitin is a 76-residue protein that serves as a protein degradation signal when conjugated to another protein. Ubiquitin has been shown to exist in at least three states: native (N-state), unfolded (U-state), and,...	nmrlearner	Journal club	0	08-21-2010 11:53 PM
[NMR paper] Secondary structure of human interleukin 2 from 3D heteronuclear NMR experiments. Secondary structure of human interleukin 2 from 3D heteronuclear NMR experiments. Related Articles Secondary structure of human interleukin 2 from 3D heteronuclear NMR experiments. Biochemistry. 1992 Aug 25;31(33):7741-4 Authors: Mott HR, Driscoll PC, Boyd J, Cooke RM, Weir MP, Campbell ID Recombinant 15N-labeled human interleukin 2 (IL-2) has been studied by 2D and 3D NMR using uniformly 15N-labeled protein. Assignment of the backbone resonances has enabled the secondary structure of the protein to be defined. The secondary structure was...	nmrlearner	Journal club	0	08-21-2010 11:45 PM
[NMR paper] Multidimensional triple resonance NMR spectroscopy of isotopically uniformly enriched Multidimensional triple resonance NMR spectroscopy of isotopically uniformly enriched proteins: a powerful new strategy for structure determination. Related Articles Multidimensional triple resonance NMR spectroscopy of isotopically uniformly enriched proteins: a powerful new strategy for structure determination. Ciba Found Symp. 1991;161:108-19; discussion 119-35 Authors: Bax A, Ikura M, Kay LE, Barbato G, Spera S A procedure is described that affords complete 1H, 13C and 15N resonance assignment in proteins of up to about 25 kDa. The new...	nmrlearner	Journal club	0	08-21-2010 11:16 PM
[NMR paper] Analysis of the backbone dynamics of interleukin-1 beta using two-dimensional inverse Analysis of the backbone dynamics of interleukin-1 beta using two-dimensional inverse detected heteronuclear 15N-1H NMR spectroscopy. Related Articles Analysis of the backbone dynamics of interleukin-1 beta using two-dimensional inverse detected heteronuclear 15N-1H NMR spectroscopy. Biochemistry. 1990 Aug 14;29(32):7387-401 Authors: Clore GM, Driscoll PC, Wingfield PT, Gronenborn AM The backbone dynamics of uniformly 15N-labeled interleukin-1 beta are investigated by using two-dimensional inverse detected heteronuclear 15N-1H NMR...	nmrlearner	Journal club	0	08-21-2010 11:04 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