NMR paper NMR experiments for resonance assignments of 13C, 15N doubly-labeled flexible polypep

		BioNMR > Educational resources > Journal club
[NMR paper] NMR experiments for resonance assignments of 13C, 15N doubly-labeled flexible polypep

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:

View First Unread

Thread Tools

Search this Thread

Rate Thread

Display Modes

11-18-2010, 09:15 PM

nmrlearner

Senior Member

Join Date: Jan 2005

Posts: 23,200

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

NMR experiments for resonance assignments of 13C, 15N doubly-labeled flexible polypep

NMR experiments for resonance assignments of 13C, 15N doubly-labeled flexible polypeptides: application to the human prion protein hPrP(23-230).

Related Articles NMR experiments for resonance assignments of 13C, 15N doubly-labeled flexible polypeptides: application to the human prion protein hPrP(23-230).

J Biomol NMR. 2000 Feb;16(2):127-38

Authors: Liu A, Riek R, Wider G, von Schroetter C, Zahn R, Wüthrich K

A combination of three heteronuclear three-dimensional NMR experiments tailored for sequential resonance assignments in uniformly 15N, 13C-labeled flexible polypeptide chains is described. The 3D (H)N(CO-TOCSY)NH, 3D (H)CA(CO-TOCSY)NH and 3D (H)CBCA(CO-TOCSY)NH schemes make use of the favorable 15N chemical shift dispersion in unfolded polypeptides, exploit the slow transverse 15N relaxation rates of unfolded polypeptides in high resolution constant-time [1H, 15N]-correlation experiments, and use carbonyl carbon homonuclear isotropic mixing to transfer magnetization sequentially along the amino acid sequence. Practical applications are demonstrated with the 100-residue flexible tail of the recombinant human prion protein, making use of spectral resolution up to 0.6 Hz in the 15N dimension, simultaneous correlation with the two adjacent amino acid residues to overcome problems associated with spectral overlap, and the potential of the presently described experiments to establish nearest-neighbor correlations across proline residues in the amino acid sequence.

PMID: 10723992 [PubMed - indexed for MEDLINE]

Source: PubMed

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
Effect of Freezing Conditions on Distances and Their Distributions Derived from Double Electron Electron Resonance (DEER): A Study of Doubly-Spin-Labeled T4 Lysozyme Effect of Freezing Conditions on Distances and Their Distributions Derived from Double Electron Electron Resonance (DEER): A Study of Doubly-Spin-Labeled T4 Lysozyme Publication year: 2012 Source: Journal of Magnetic Resonance, Available online 24 January 2012</br> Elka R.Georgieva, Aritro S.Roy, Vladimir M.Grigoryants, Petr P.Borbat, Keith A.*Earle, ...</br> Pulsed dipolar ESR spectroscopy, DEER and DQC, require frozen samples. An important issue in the biological application of this technique is how the freezing rate and concentration of cryoprotectant could possibly affect the...	nmrlearner	Journal club	0	01-25-2012 08:56 AM
Multidimensional oriented solid-state NMR experiments enable the sequential assignment of uniformly 15N labeled integral membrane proteins in magnetically aligned lipid bilayers Multidimensional oriented solid-state NMR experiments enable the sequential assignment of uniformly 15N labeled integral membrane proteins in magnetically aligned lipid bilayers Abstract Oriented solid-state NMR is the most direct methodology to obtain the orientation of membrane proteins with respect to the lipid bilayer. The method consists of measuring 1H-15N dipolar couplings (DC) and 15N anisotropic chemical shifts (CSA) for membrane proteins that are uniformly aligned with respect to the membrane bilayer. A significant advantage of this approach is that tilt and azimuthal...	nmrlearner	Journal club	0	10-10-2011 06:27 AM
[NMR paper] Expression of doubly labeled Saccharomyces cerevisiae iso-1 ferricytochrome c and (1) Expression of doubly labeled Saccharomyces cerevisiae iso-1 ferricytochrome c and (1)H, (13)C and (15)N chemical shift assignments by multidimensional NMR. Related Articles Expression of doubly labeled Saccharomyces cerevisiae iso-1 ferricytochrome c and (1)H, (13)C and (15)N chemical shift assignments by multidimensional NMR. FEBS Lett. 2000 Sep 29;482(1-2):25-30 Authors: Szabo CM, Sanders LK, Le HC, Chien EY, Oldfield E We have expressed -labeled Saccharomyces cerevisiae iso-1 cytochrome c C102T;K72A in Escherichia coli with a yield of 11...	nmrlearner	Journal club	0	11-19-2010 08:29 PM
[NMR paper] NMR with 13C, 15N-doubly-labeled DNA: the Antennapedia homeodomain complex with a 14- NMR with 13C, 15N-doubly-labeled DNA: the Antennapedia homeodomain complex with a 14-mer DNA duplex. NMR with 13C, 15N-doubly-labeled DNA: the Antennapedia homeodomain complex with a 14-mer DNA duplex. J Biomol NMR. 1998 Jul;12(1):25-37 Authors: Fernández C, Szyperski T, Ono A, Iwai H, Tate S, Kainosho M, Wüthrich K Nearly complete 1H, 13C and 15N NMR assignments have been obtained for a doubly labeled 14-base pair DNA duplex in solution both in the free state and complexed with the uniformly 15N-labeled Antennapedia homeodomain. The DNA was...	nmrlearner	Journal club	0	11-17-2010 11:15 PM
High-resolution methyl edited GFT NMR experiments for protein resonance assignments a High-resolution methyl edited GFT NMR experiments for protein resonance assignments and structure determination Abstract Three-dimensional (3D) structure determination of proteins is benefitted by long-range distance constraints comprising the methyl groups, which constitute the hydrophobic core of proteins. However, in methyl groups (of Ala, Ile, Leu, Met, Thr and Val) there is a significant overlap of 13C and 1H chemical shifts. Such overlap can be resolved using the recently proposed (3,2)D HCCH-COSY, a G-matrix Fourier transform (GFT) NMR based experiment, which facilitates editing...	nmrlearner	Journal club	0	09-18-2010 04:53 AM
High-resolution methyl edited GFT NMR experiments for protein resonance assignments a High-resolution methyl edited GFT NMR experiments for protein resonance assignments and structure determination. Related Articles High-resolution methyl edited GFT NMR experiments for protein resonance assignments and structure determination. J Biomol NMR. 2010 Sep 14; Authors: Jaipuria G, Thakur A, D'Silva P, Atreya HS Three-dimensional (3D) structure determination of proteins is benefitted by long-range distance constraints comprising the methyl groups, which constitute the hydrophobic core of proteins. However, in methyl groups (of Ala, Ile,...	nmrlearner	Journal club	0	09-15-2010 02:26 PM
[NMR paper] 15N NMR assignments and chemical shift analysis of uniformly labeled 15N calbindin D9 15N NMR assignments and chemical shift analysis of uniformly labeled 15N calbindin D9k in the apo, (Cd2+)1 and (Ca2+)2 states. Related Articles 15N NMR assignments and chemical shift analysis of uniformly labeled 15N calbindin D9k in the apo, (Cd2+)1 and (Ca2+)2 states. FEBS Lett. 1992 Jun 1;303(2-3):136-40 Authors: Skelton NJ, Akke M, KÃ¶rdel J, Thulin E, ForsÃ©n S, Chazin WJ 15N has been uniformly incorporated into the EF-hand Ca(2+)-binding protein calbindin D9k so that heteronuclear experiments can be used to further characterize the...	nmrlearner	Journal club	0	08-21-2010 11:41 PM
Nitrogen-detected CAN and CON experiments as alternative experiments for main chain N Abstract Heteronuclear direct-detection experiments, which utilize the slower relaxation properties of low Î³ nuclei, such as 13C have recently been proposed for sequence-specific assignment and structural analyses of large, unstructured, and/or paramagnetic proteins. Here we present two novel 15N direct-detection experiments. The CAN experiment sequentially connects amide 15N resonances using 13CÎ± chemical shift matching, and the CON experiment connects the preceding 13Câ?² nuclei. When starting from the same carbon polarization, the intensities of nitrogen signals detected in the CAN or...	nmrlearner	Journal club	0	08-14-2010 04:19 AM

« 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