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  
Old 11-24-2010, 08:58 PM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 23,734
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 NMR structure determination and investigation using a reduced proton (REDPRO) labelin

NMR structure determination and investigation using a reduced proton (REDPRO) labeling strategy for proteins.

Related Articles NMR structure determination and investigation using a reduced proton (REDPRO) labeling strategy for proteins.

FEBS Lett. 2002 Jul 31;524(1-3):177-82

Authors: Shekhtman A, Ghose R, Goger M, Cowburn D

We present here a stable isotope labeling technique for proteins, which seeks the appropriate compromise between the advantages of (a) random isotope labeling, with its large number of protons available for structure determination, and (b) selective labeling to generate isolated proton spins decreasing spectral complexity and improving relaxation properties of NMR experiments. The described reduced proton (REDPRO) procedure results in side-chain specific protonation of overexpressed proteins, which is highly selective. The REDPRO labeling scheme provides a sufficient number of NOE constraints for structure calculation. Dramatically improved relaxation properties of the heteronuclear magnetization transfer coupled with TROSY advantages make the proposed labeling scheme an attractive approach for study of high molecular weight protein targets, their ligand sites, and interdomain interactions.

PMID: 12135763 [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
A Proton-Detected 4D Solid-State NMR Experiment for Protein Structure Determination.
A Proton-Detected 4D Solid-State NMR Experiment for Protein Structure Determination. A Proton-Detected 4D Solid-State NMR Experiment for Protein Structure Determination. Chemphyschem. 2011 Apr 4;12(5):915-8 Authors: Huber M, Hiller S, Schanda P, Ernst M, Böckmann A, Verel R, Meier BH
nmrlearner Journal club 0 03-29-2011 07:04 PM
[NMR paper] A proton-NMR investigation of the fully reduced cytochrome c7 from Desulfuromonas ace
A proton-NMR investigation of the fully reduced cytochrome c7 from Desulfuromonas acetoxidans. Comparison between the reduced and the oxidized forms. Related Articles A proton-NMR investigation of the fully reduced cytochrome c7 from Desulfuromonas acetoxidans. Comparison between the reduced and the oxidized forms. Eur J Biochem. 1999 Dec;266(2):634-43 Authors: Assfalg M, Banci L, Bertini I, Bruschi M, Giudici-Orticoni MT, Turano P The solution structure via 1H NMR of the fully reduced form of cytochrome c7 has been obtained. The protein...
nmrlearner Journal club 0 11-18-2010 08:31 PM
[NMR paper] Proton NMR investigation of the heme active site structure of an engineered cytochrom
Proton NMR investigation of the heme active site structure of an engineered cytochrome c peroxidase that mimics manganese peroxidase. Related Articles Proton NMR investigation of the heme active site structure of an engineered cytochrome c peroxidase that mimics manganese peroxidase. Biochemistry. 1999 Jul 13;38(28):9146-57 Authors: Wang X, Lu Y The heme active site structure of an engineered cytochrome c peroxidase that closely mimics manganese peroxidase (MnP) has been characterized by both one- and two-dimensional NMR spectroscopy. All...
nmrlearner Journal club 0 11-18-2010 08:31 PM
[NMR paper] Proton NMR investigation of the [4Fe--4S]1+ cluster environment of nitrogenase iron p
Proton NMR investigation of the 1+ cluster environment of nitrogenase iron protein from Azotobacter vinelandii: defining nucleotide-induced conformational changes. Related Articles Proton NMR investigation of the 1+ cluster environment of nitrogenase iron protein from Azotobacter vinelandii: defining nucleotide-induced conformational changes. Biochemistry. 1995 Dec 5;34(48):15646-53 Authors: Lanzilotta WN, Holz RC, Seefeldt LC This work presents the complete assignment of the isotropically shifted 1H NMR resonances of Azotobacter vinelandii...
nmrlearner Journal club 0 08-22-2010 03:50 AM
[NMR paper] Proton NMR investigation of substrate-bound heme oxygenase: evidence for electronic a
Proton NMR investigation of substrate-bound heme oxygenase: evidence for electronic and steric contributions to stereoselective heme cleavage. Related Articles Proton NMR investigation of substrate-bound heme oxygenase: evidence for electronic and steric contributions to stereoselective heme cleavage. Biochemistry. 1994 May 31;33(21):6631-41 Authors: Hernández G, Wilks A, Paolesse R, Smith KM, Ortiz de Montellano PR, La Mar GN The substrate-bound form of the enzyme heme oxygenase (HO), which catalyzed the stereospecific alpha-meso bridge...
nmrlearner Journal club 0 08-22-2010 03:33 AM
[NMR paper] Proton NMR investigation of substrate-bound heme oxygenase: evidence for electronic a
Proton NMR investigation of substrate-bound heme oxygenase: evidence for electronic and steric contributions to stereoselective heme cleavage. Related Articles Proton NMR investigation of substrate-bound heme oxygenase: evidence for electronic and steric contributions to stereoselective heme cleavage. Biochemistry. 1994 May 31;33(21):6631-41 Authors: Hernández G, Wilks A, Paolesse R, Smith KM, Ortiz de Montellano PR, La Mar GN The substrate-bound form of the enzyme heme oxygenase (HO), which catalyzed the stereospecific alpha-meso bridge...
nmrlearner Journal club 0 08-22-2010 03:33 AM
[NMR paper] 1H-NMR investigation of oxidized and reduced high-potential iron-sulfur protein from
1H-NMR investigation of oxidized and reduced high-potential iron-sulfur protein from Rhodopseudomonas globiformis. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles 1H-NMR investigation of oxidized and reduced high-potential iron-sulfur protein from Rhodopseudomonas globiformis. Eur J Biochem. 1993 Feb 15;212(1):69-78 Authors: Bertini I, Capozzi F, Luchinat C, Piccioli M 1H one-dimensional and two-dimensional NMR spectra have been...
nmrlearner Journal club 0 08-21-2010 11:53 PM
[NMR paper] Comparison of amide proton exchange in reduced and oxidized Rhodobacter capsulatus cy
Comparison of amide proton exchange in reduced and oxidized Rhodobacter capsulatus cytochrome c2: a 1H-15N NMR study. Related Articles Comparison of amide proton exchange in reduced and oxidized Rhodobacter capsulatus cytochrome c2: a 1H-15N NMR study. J Biomol NMR. 1991 Jul;1(2):145-54 Authors: Gooley PR, Zhao D, MacKenzie NE The hydrogen-deuterium exchange rates of the reduced and oxidized forms of Rhodobacter capsulatus cytochrome c2 were studied by 1H-15N homonuclear multiple quantum correlation spectroscopy. Minimal differences were...
nmrlearner Journal club 0 08-21-2010 11:16 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 09:50 PM.


Map