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
Home Forums Wiki NMR feeds Downloads Register Today's Posts



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, 10:03 PM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 23,174
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 Addressing the overlap problem in the quantitative analysis of two dimensional NMR sp

Addressing the overlap problem in the quantitative analysis of two dimensional NMR spectra: application to (15)N relaxation measurements.

Related Articles Addressing the overlap problem in the quantitative analysis of two dimensional NMR spectra: application to (15)N relaxation measurements.

J Biomol NMR. 2004 Nov;30(3):347-52

Authors: Tugarinov V, Choy WY, Kupce E, Kay LE

A quantitative analysis of 2D (1)H-(15)N spectra is often complicated by resonance overlap. Here a simple method is presented for resolving overlapped correlations by recording 2D projection planes from HNCO data sets. Applications are presented involving the measurement of (15)N T(1rho) relaxation rates in a high molecular weight protein, malate synthase G, and in a system that exchanges between folded and unfolded states, the drkN SH3 domain. By supplementing relaxation data recorded in the conventional way as a series of 2D (1)H-(15)N data sets with a series of a pair of projection planes the number of dynamics probes is increased significantly for both systems studied.

PMID: 15756461 [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
Conformational analysis by quantitative NOE measurements of the β-proton pairs across individual disulfide bonds in proteins
Conformational analysis by quantitative NOE measurements of the β-proton pairs across individual disulfide bonds in proteins Abstract NOEs between the β-protons of cysteine residues across disulfide bonds in proteins provide direct information on the connectivities and conformations of these important cross-links, which are otherwise difficult to investigate. With conventional -proteins, however, fast spin diffusion processes mediated by strong dipolar interactions between geminal β-protons prohibit the quantitative measurements and thus the analyses of long-range NOEs across...
nmrlearner Journal club 0 12-05-2011 04:07 AM
A rigid disulfide-linked nitroxide side chain simplifies the quantitative analysis of PRE data
A rigid disulfide-linked nitroxide side chain simplifies the quantitative analysis of PRE data Abstract The measurement of 1H transverse paramagnetic relaxation enhancement (PRE) has been used in biomolecular systems to determine long-range distance restraints and to visualize sparsely-populated transient states. The intrinsic flexibility of most nitroxide and metal-chelating paramagnetic spin-labels, however, complicates the quantitative interpretation of PREs due to delocalization of the paramagnetic center. Here, we present a novel, disulfide-linked nitroxide spin label, R1p, as...
nmrlearner Journal club 0 09-30-2011 08:01 PM
Protein Analysis by (31)P NMR Spectroscopy in Ionic Liquid: Quantitative Determination of Enzymatically Created Cross-Links.
Protein Analysis by (31)P NMR Spectroscopy in Ionic Liquid: Quantitative Determination of Enzymatically Created Cross-Links. Protein Analysis by (31)P NMR Spectroscopy in Ionic Liquid: Quantitative Determination of Enzymatically Created Cross-Links. J Agric Food Chem. 2011 Jan 10; Authors: Monogioudi E, Permi P, Filpponen I, Lienemann M, Li B, Argyropoulos D, Buchert J, Mattinen ML Cross-linking of ?-casein by Trichoderma reesei tyrosinase (TrTyr) and Streptoverticillium mobaraense transglutaminase (Tgase) was analyzed by (31)P nuclear magnetic...
nmrlearner Journal club 0 01-12-2011 11:11 AM
[NMR paper] Inverse methods in two-dimensional NMR spectral analysis.
Inverse methods in two-dimensional NMR spectral analysis. Related Articles Inverse methods in two-dimensional NMR spectral analysis. J Magn Reson. 2003 May;162(1):141-57 Authors: van Beek JD, Meier BH, Schäfer H Solid-state NMR is a valuable technique for the study of disordered materials. Analysis of such spectra usually involves solution of so-called ill-posed inverse problems. Here we present a strategy for the analysis of two-parameter two-dimensional NMR problems and test it on 2D DECODER and DOQSY experiments. Using Monte Carlo tests,...
nmrlearner Journal club 0 11-24-2010 09:01 PM
Quantitative Analysis of Protein Backbone Dynamics in Microcrystalline Ubiquitin by S
Quantitative Analysis of Protein Backbone Dynamics in Microcrystalline Ubiquitin by Solid-State NMR Spectroscopy. Related Articles Quantitative Analysis of Protein Backbone Dynamics in Microcrystalline Ubiquitin by Solid-State NMR Spectroscopy. J Am Chem Soc. 2010 Oct 26; Authors: Schanda P, Meier BH, Ernst M Characterization of protein dynamics by solid-state NMR spectroscopy requires robust and accurate measurement protocols, which are not yet fully developed. In this study, we investigate the backbone dynamics of microcrystalline ubiquitin...
nmrlearner Journal club 0 10-29-2010 07:05 PM
Quantitative Analysis of Protein Backbone Dynamics in Microcrystalline Ubiquitin by S
Quantitative Analysis of Protein Backbone Dynamics in Microcrystalline Ubiquitin by Solid-State NMR Spectroscopy Paul Schanda, Beat H. Meier and Matthias Ernst http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja100726a/aop/images/medium/ja-2010-00726a_0001.gif Journal of the American Chemical Society DOI: 10.1021/ja100726a http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA http://feeds.feedburner.com/~r/acs/jacsat/~4/vMvBmzNs148
nmrlearner Journal club 0 10-26-2010 08:48 PM
[NMR paper] Quantitative analysis of 1H NMR detected proteins in the rat cerebral cortex in vivo
Quantitative analysis of 1H NMR detected proteins in the rat cerebral cortex in vivo and in vitro. Related Articles Quantitative analysis of 1H NMR detected proteins in the rat cerebral cortex in vivo and in vitro. NMR Biomed. 1993 Jul-Aug;6(4):242-7 Authors: Kauppinen RA, Niskanen T, Hakumäki J, Williams SR Spectral editing experiments were used to quantify CH3 groups from macromolecular species in the chemical shift region from 1.2 to 1.4 ppm of rat cerebrum in vivo. Two peaks centred at 1.22 and 1.40 ppm were revealed when irradiation was...
nmrlearner Journal club 0 08-21-2010 11:53 PM
[NMR analysis blog] Fighting against peak overlap – Introducing Global Spectral Deconvolution (GSD)
Fighting against peak overlap – Introducing Global Spectral Deconvolution (GSD) 1H NMR is for sure the most powerful technique for structure elucidation, especially for small organic molecules. Typically, an organic chemist uses the chemical shift, coupling constants and integration information contained in an 1H-NMR spectrum to either verify or elucidate an unknown compound. Of course, it’s quite common that a simple 1H-NMR spectrum is not enough to unambiguously confirm a structure and thus other NMR experiments (e.g. 13C-NMR, HSQC, COSY, etc) are used to get more structural information....
nmrlearner News from NMR blogs 0 08-21-2010 09:12 PM



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 10:29 AM.


Map