BioNMR
NMR aggregator & online community since 2003
BioNMR    
Learn or help to learn NMR - get free NMR books!
 

Go Back   BioNMR > Educational resources > Journal club
Advanced Search



Jobs Groups Conferences Literature Pulse sequences Software forums Programs Sample preps Web resources BioNMR issues


Webservers
NMR processing:
MDD
NMR assignment:
Backbone:
Autoassign
MARS
UNIO Match
PINE
Side-chains:
UNIO ATNOS-Ascan
NOEs:
UNIO ATNOS-Candid
UNIO Candid
ASDP
Structure from NMR restraints:
Ab initio:
GeNMR
Cyana
XPLOR-NIH
ASDP
UNIO ATNOS-Candid
UNIO Candid
Fragment-based:
BMRB CS-Rosetta
Rosetta-NMR (Robetta)
Template-based:
GeNMR
I-TASSER
Refinement:
Amber
Structure from chemical shifts:
Fragment-based:
WeNMR CS-Rosetta
BMRB CS-Rosetta
Homology-based:
CS23D
Simshift
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:
Shiftcor
UNIO Shiftinspector
LACS
CheckShift
RefDB
NMR model quality:
NOEs, other restraints:
PROSESS
PSVS
RPF scores
iCing
Chemical shifts:
PROSESS
CheShift2
Vasco
iCing
RDCs:
DC
Anisofit
Pseudocontact shifts:
Anisofit
Protein geomtery:
Resolution-by-Proxy
PROSESS
What-If
iCing
PSVS
MolProbity
SAVES2 or SAVES4
Vadar
Prosa
ProQ
MetaMQAPII
PSQS
Eval123D
STAN
Ramachandran Plot
Rampage
ERRAT
Verify_3D
Harmony
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:
camLILA
ccSOL
Camfold
camGroEL
Zyggregator
Isotope labeling:
UPLABEL
Solid-state NMR:
sedNMR


Reply
Thread Tools Search this Thread Rate Thread Display Modes
  #1  
Unread 11-24-2010, 09:51 PM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 23,134
Points: 193,617, Level: 100
Points: 193,617, Level: 100 Points: 193,617, Level: 100 Points: 193,617, Level: 100
Level up: 0%, 0 Points needed
Level up: 0% Level up: 0% Level up: 0%
Activity: 50.7%
Activity: 50.7% Activity: 50.7% Activity: 50.7%
Last Achievements
Award-Showcase
NMR Credits: 0
NMR Points: 193,617
Downloads: 0
Uploads: 0
Default Combined frequency- and time-domain NMR spectroscopy. Application to fast protein res

Combined frequency- and time-domain NMR spectroscopy. Application to fast protein resonance assignment.

Related Articles Combined frequency- and time-domain NMR spectroscopy. Application to fast protein resonance assignment.

J Biomol NMR. 2004 May;29(1):57-64

Authors: Brutscher B

A simple and general method is presented to simplify multi-dimensional NMR spectra of isotope-labeled bio-molecules. The approach is based on band-selective Hadamard-type frequency encoding, which disperses the correlation peaks into different sub-spectra. This makes it possible to apply low-dimensionality-based NMR techniques to larger molecular systems. Here we demonstrate the use of band-selective Hadamard frequency labeling for fast protein resonance assignment, based on our recently proposed suite of 2D experiments (Bersch et al., 2003).

PMID: 15017139 [PubMed - indexed for MEDLINE]



Source: PubMed
Reply With Quote


Did you find this post helpful? Yes | No

Reply
Similar Threads
Thread Thread Starter Forum Replies Last Post
Application of iterative soft thresholding for fast reconstruction of NMR data non-uniformly sampled with multidimensional Poisson Gap scheduling
Application of iterative soft thresholding for fast reconstruction of NMR data non-uniformly sampled with multidimensional Poisson Gap scheduling Abstract The fast Fourier transformation has been the gold standard for transforming data from time to frequency domain in many spectroscopic methods, including NMR. While reliable, it has as a drawback that it requires a grid of uniformly sampled data points. This needs very long measuring times for sampling in multidimensional experiments in all indirect dimensions uniformly and even does not allow reaching optimal evolution times that would...
nmrlearner Journal club 0 02-16-2012 05:24 AM
Paramagnetic relaxation enhancement to improve sensitivity of fast NMR methods: application to intrinsically disordered proteins
Paramagnetic relaxation enhancement to improve sensitivity of fast NMR methods: application to intrinsically disordered proteins Abstract We report enhanced sensitivity NMR measurements of intrinsically disordered proteins in the presence of paramagnetic relaxation enhancement (PRE) agents such as Ni2+-chelated DO2A. In proton-detected 1H-15N SOFAST-HMQC and carbon-detected (H-flip)13CO-15N experiments, faster longitudinal relaxation enables the usage of even shorter interscan delays. This results in higher NMR signal intensities per units of experimental time, without adverse line...
nmrlearner Journal club 0 10-21-2011 10:04 PM
[NMR paper] Very fast two-dimensional NMR spectroscopy for real-time investigation of dynamic eve
Very fast two-dimensional NMR spectroscopy for real-time investigation of dynamic events in proteins on the time scale of seconds. Related Articles Very fast two-dimensional NMR spectroscopy for real-time investigation of dynamic events in proteins on the time scale of seconds. J Am Chem Soc. 2005 Jun 8;127(22):8014-5 Authors: Schanda P, Brutscher B We demonstrate for different protein samples that 2D 1H-15N correlation NMR spectra can be recorded in a few seconds of acquisition time using a new band-selective optimized flip-angle...
nmrlearner Journal club 0 11-25-2010 08:21 PM
[NMR paper] Fast mapping of protein-protein interfaces by NMR spectroscopy.
Fast mapping of protein-protein interfaces by NMR spectroscopy. Related Articles Fast mapping of protein-protein interfaces by NMR spectroscopy. J Am Chem Soc. 2003 Nov 26;125(47):14250-1 Authors: Reese ML, Dötsch V Identifying the interface of protein complexes can represent a difficult task in structural biology. Here, we report a method for the fast mapping of interfaces of protein complexes by NMR without the need for the assignments of the proteins involved.
nmrlearner Journal club 0 11-24-2010 09:16 PM
[NMR paper] Real-time and equilibrium (19)F-NMR studies reveal the role of domain-domain interact
Real-time and equilibrium (19)F-NMR studies reveal the role of domain-domain interactions in the folding of the chaperone PapD. Related Articles Real-time and equilibrium (19)F-NMR studies reveal the role of domain-domain interactions in the folding of the chaperone PapD. Proc Natl Acad Sci U S A. 2002 Jan 22;99(2):709-14 Authors: Bann JG, Pinkner J, Hultgren SJ, Frieden C PapD is a periplasmic chaperone essential for P pilus formation in pyelonephritic strains of E. coli. It is composed of two domains, each of which contains a tryptophan...
nmrlearner Journal club 0 11-24-2010 08:49 PM
[NMR paper] Folding kinetics of the SH3 domain of PI3 kinase by real-time NMR combined with optic
Folding kinetics of the SH3 domain of PI3 kinase by real-time NMR combined with optical spectroscopy. Related Articles Folding kinetics of the SH3 domain of PI3 kinase by real-time NMR combined with optical spectroscopy. J Mol Biol. 1998 Feb 27;276(3):657-67 Authors: Guijarro JI, Morton CJ, Plaxco KW, Campbell ID, Dobson CM The refolding kinetics of the chemically denatured SH3 domain of phosphatidylinositol 3'-kinase (PI3-SH3) have been monitored by real-time one-dimensional 1H NMR coupled with a variety of other biophysical techniques. These...
nmrlearner Journal club 0 11-17-2010 11:06 PM
[NMR paper] Following protein folding in real time using NMR spectroscopy.
Following protein folding in real time using NMR spectroscopy. Related Articles Following protein folding in real time using NMR spectroscopy. Nat Struct Biol. 1995 Oct;2(10):865-70 Authors: Balbach J, Forge V, van Nuland NA, Winder SL, Hore PJ, Dobson CM The refolding of apo bovine alpha-lactalbumin has been monitored in real time by NMR spectroscopy following rapid in situ dilution of a chemically denatured state. By examining individual resonances in the time-resolved NMR spectra, the native state has been shown to emerge in a cooperative...
nmrlearner Journal club 0 08-22-2010 03:50 AM
Simultaneous detection of amide and methyl correlations using a time shared NMR experiment: application to binding epitope mapping
Simultaneous detection of amide and methyl correlations using a time shared NMR experiment: application to binding epitope mapping Peter Würtz, Olli Aitio, Maarit Hellman and Perttu Permi Journal of Biomolecular NMR; 2007; 39(2) pp 97 - 105 Abstract: Simultaneous recording of different NMR parameters is an efficient way to reduce the overall experimental time and speed up structural studies of biological macromolecules. This can especially be beneficial in the case of fast NMR-based drug screening applications or for collecting NOE restraints, where prohibitively long data collection...
stewart Journal club 0 08-05-2008 01:41 PM


Thread Tools Search this Thread
Search this Thread:

Advanced Search
Display Modes Rate This Thread
Rate This 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



BioNMR advertisements to pay for website hosting and domain registration. Nobody does it for us.



Powered by vBulletin® Version 3.7.3
Copyright ©2000 - 2024, Jelsoft Enterprises Ltd.
Copyright, BioNMR.com, 2003-2013
Search Engine Friendly URLs by vBSEO 3.6.0

All times are GMT. The time now is 11:31 AM.


Map