NMR paper Double and triple resonance NMR methods for protein assignment.

		BioNMR > Educational resources > Journal club
[NMR paper] Double and triple resonance NMR methods for protein assignment.

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

08-22-2010, 03:31 PM

nmrlearner

Senior Member

Join Date: Jan 2005

Posts: 23,780

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

Double and triple resonance NMR methods for protein assignment.

Double and triple resonance NMR methods for protein assignment.

Related Articles Double and triple resonance NMR methods for protein assignment.

Methods Mol Biol. 1997;60:29-52

Authors: Whitehead B, Craven CJ, Waltho JP

PMID: 9276245 [PubMed - indexed for MEDLINE]

Source: PubMed

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
Combinatorial triple-selective labeling as a tool to assist membrane protein backbone resonance assignment Combinatorial triple-selective labeling as a tool to assist membrane protein backbone resonance assignment Abstract Obtaining NMR assignments for slowly tumbling molecules such as detergent-solubilized membrane proteins is often compromised by low sensitivity as well as spectral overlap. Both problems can be addressed by amino-acid specific isotope labeling in conjunction with 15Nâ??1H correlation experiments. In this work an extended combinatorial selective in vitro labeling scheme is proposed that seeks to reduce the number of samples required for assignment. Including three...	nmrlearner	Journal club	0	01-21-2012 06:26 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. 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
Pseudo-4D triple resonance experiments to resolve HN overlap in the backbone assignment of unfolded proteins Pseudo-4D triple resonance experiments to resolve HN overlap in the backbone assignment of unfolded proteins Abstract The solution NMR resonance assignment of the protein backbone is most commonly carried out using triple resonance experiments that involve 15N and 1HN resonances. The assignment becomes problematic when there is resonance overlap of 15Nâ??1HN cross peaks. For such residues, one cannot unambiguously link the â??leftâ?? side of the NH root to the â??rightâ?? side, and the residues associated with such overlapping HN resonances remain often unassigned. Here we present a...	nmrlearner	Journal club	0	12-31-2010 08:38 PM
[NMR paper] Closed form of liganded glutamine-binding protein by rotational-echo double-resonance Closed form of liganded glutamine-binding protein by rotational-echo double-resonance NMR. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Closed form of liganded glutamine-binding protein by rotational-echo double-resonance NMR. Biochemistry. 1997 Aug 5;36(31):9405-8 Authors: Klug CA, Tasaki K, Tjandra N, Ho C, Schaefer J Rotational-echo double-resonance NMR has been used to determine internuclear distances in the complex of glutamine-binding protein and its ligand, l-glutamine. The...	nmrlearner	Journal club	0	08-22-2010 05:08 PM
[NMR paper] Double and triple resonance NMR methods for protein assignment. Double and triple resonance NMR methods for protein assignment. Related Articles Double and triple resonance NMR methods for protein assignment. Methods Mol Biol. 1997;60:29-52 Authors: Whitehead B, Craven CJ, Waltho JP	nmrlearner	Journal club	0	08-22-2010 03:03 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
[NMR paper] Solid-state NMR triple-resonance backbone assignments in a protein. Solid-state NMR triple-resonance backbone assignments in a protein. Related Articles Solid-state NMR triple-resonance backbone assignments in a protein. J Biomol NMR. 1999 Apr;13(4):337-42 Authors: Tan WM, Gu Z, Zeri AC, Opella SJ Triple-resonance solid-state NMR spectroscopy is demonstrated to sequentially assign the 13C' and 15N amide backbone resonances of adjacent residues in an oriented protein sample. The observed 13C' chemical shift frequency provides an orientational constraint complementary to those measured from the 1H and 15N amide...	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