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, 08:58 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 Longitudinal (1)H relaxation optimization in TROSY NMR spectroscopy.

Longitudinal (1)H relaxation optimization in TROSY NMR spectroscopy.

Related Articles Longitudinal (1)H relaxation optimization in TROSY NMR spectroscopy.

J Am Chem Soc. 2002 Oct 30;124(43):12898-902

Authors: Pervushin K, Vögeli B, Eletsky A

A general method to enhance the sensitivity of the multidimensional NMR experiments performed at high-polarizing magnetic field via the significant reduction of the longitudinal proton relaxation times is described. The method is based on the use of two vast pools of "thermal bath" 1H spins residing on hydrogens covalently attached to carbon and oxygen atoms in 13C,15N labeled and fully protonated or fractionally deuterated proteins to uniformly enhance longitudinal relaxation of the 1HN spins and concomitantly the sensitivity of multipulse NMR experiments. The proposed longitudinal relaxation optimization is implemented in the 2D [15N,1H]-LTROSY, 2D [15N,1H]-LHSQC and 3D LTROSY-HNCA experiments yielding the factor 2-2.5 increase of the maximal signal-to-noise ratio per unit time at 600 MHz. At 900 MHz, the predicted decrease of the 1HN longitudinal relaxation times can be as large as one order of magnitude, making the proposed method an important tool for protein NMR at high magnetic fields.

PMID: 12392438 [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
Evaluation of the influence of intermolecular electron-nucleus couplings and intrinsic metal binding sites on the measurement of 15N longitudinal paramagnetic relaxation enhancements in proteins by solid-state NMR
Evaluation of the influence of intermolecular electron-nucleus couplings and intrinsic metal binding sites on the measurement of 15N longitudinal paramagnetic relaxation enhancements in proteins by solid-state NMR Abstract Magic-angle spinning solid-state NMR measurements of 15N longitudinal paramagnetic relaxation enhancements (PREs) in 13C,15N-labeled proteins modified with Cu2+-chelating tags can yield multiple long-range electron-nucleus distance restraints up to ~20 Ă? (Nadaud et al. in J Am Chem Soc 131:8108â??8120, 2009). Using the EDTA-Cu2+ K28C mutant of B1 immunoglobulin...
nmrlearner Journal club 0 08-13-2011 02:47 AM
Evaluation of the influence of intermolecular electron-nucleus couplings and intrinsic metal binding sites on the measurement of (15)N longitudinal paramagnetic relaxation enhancements in proteins by solid-state NMR.
Evaluation of the influence of intermolecular electron-nucleus couplings and intrinsic metal binding sites on the measurement of (15)N longitudinal paramagnetic relaxation enhancements in proteins by solid-state NMR. Evaluation of the influence of intermolecular electron-nucleus couplings and intrinsic metal binding sites on the measurement of (15)N longitudinal paramagnetic relaxation enhancements in proteins by solid-state NMR. J Biomol NMR. 2011 Aug 9; Authors: Nadaud PS, Sengupta I, Helmus JJ, Jaroniec CP Magic-angle spinning solid-state NMR...
nmrlearner Journal club 0 08-10-2011 12:30 PM
Optimization of NMR spectroscopy of encapsulated proteins dissolved in low viscosity fluids
Optimization of NMR spectroscopy of encapsulated proteins dissolved in low viscosity fluids Abstract Comprehensive application of solution NMR spectroscopy to studies of macromolecules remains fundamentally limited by the molecular rotational correlation time. For proteins, molecules larger than 30 kDa require complex experimental methods, such as TROSY in conjunction with isotopic labeling schemes that are often expensive and generally reduce the potential information available. We have developed the reverse micelle encapsulation strategy as an alternative approach. Encapsulation of...
nmrlearner Journal club 0 07-15-2011 09:10 PM
Optimization of NMR spectroscopy of encapsulated proteins dissolved in low viscosity fluids.
Optimization of NMR spectroscopy of encapsulated proteins dissolved in low viscosity fluids. Optimization of NMR spectroscopy of encapsulated proteins dissolved in low viscosity fluids. J Biomol NMR. 2011 Jul 12; Authors: Nucci NV, Marques BS, Bédard S, Dogan J, Gledhill JM, Moorman VR, Peterson RW, Valentine KG, Wand AL, Wand AJ Comprehensive application of solution NMR spectroscopy to studies of macromolecules remains fundamentally limited by the molecular rotational correlation time. For proteins, molecules larger than 30*kDa require complex...
nmrlearner Journal club 0 07-13-2011 06:42 PM
Elucidating slow binding kinetics of a protein without observable bound resonances by longitudinal relaxation NMR spectroscopy
Elucidating slow binding kinetics of a protein without observable bound resonances by longitudinal relaxation NMR spectroscopy Abstract We developed a new method to elucidate the binding kinetics kon and koff, and the dissociation constant KD (=koff/kon), of protein-protein interactions without observable bound resonances of the protein of interest due to high molecular weight in a complex with a large target protein. In our method, kon and koff rates are calculated from the analysis of longitudinal relaxation rates of free resonances measured for multiple samples containing different...
nmrlearner Journal club 0 06-06-2011 12:53 AM
Elucidating slow binding kinetics of a protein without observable bound resonances by longitudinal relaxation NMR spectroscopy.
Elucidating slow binding kinetics of a protein without observable bound resonances by longitudinal relaxation NMR spectroscopy. Elucidating slow binding kinetics of a protein without observable bound resonances by longitudinal relaxation NMR spectroscopy. J Biomol NMR. 2011 May 28; Authors: Sugase K We developed a new method to elucidate the binding kinetics k(on) and k(off), and the dissociation constant K(D) (=k(off)/k(on)), of protein-protein interactions without observable bound resonances of the protein of interest due to high molecular...
nmrlearner Journal club 0 06-01-2011 02:30 PM
[NMR paper] NMR spectroscopic detection of protein protons and longitudinal relaxation rates betw
NMR spectroscopic detection of protein protons and longitudinal relaxation rates between 0.01 and 50 MHz. Related Articles NMR spectroscopic detection of protein protons and longitudinal relaxation rates between 0.01 and 50 MHz. Angew Chem Int Ed Engl. 2005 Apr 8;44(15):2223-5 Authors: Bertini I, Gupta YK, Luchinat C, Parigi G, Schlörb C, Schwalbe H
nmrlearner Journal club 0 11-25-2010 08:21 PM
[NMR paper] Optimization of three-dimensional TROSY-type HCCH NMR correlation of aromatic (1)H-(1
Optimization of three-dimensional TROSY-type HCCH NMR correlation of aromatic (1)H-(13)C groups in proteins. Related Articles Optimization of three-dimensional TROSY-type HCCH NMR correlation of aromatic (1)H-(13)C groups in proteins. J Magn Reson. 1999 Aug;139(2):447-50 Authors: Meissner A, Sorensen OW Improved methods for three-dimensional TROSY-Type HCCH correlation involving protons of negligible CSA are presented. The TROSY approach differs from the conventional approach of heteronuclear decoupling in evolution and detection periods by...
nmrlearner Journal club 0 11-18-2010 08:31 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 02:14 PM.


Map