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 11-25-2010, 08:21 PM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 23,617
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 backbone assignment of the mitogen-activated protein (MAP) kinase p38.

NMR backbone assignment of the mitogen-activated protein (MAP) kinase p38.

Related Articles NMR backbone assignment of the mitogen-activated protein (MAP) kinase p38.

J Biomol NMR. 2005 Jun;32(2):175

Authors: Vogtherr M, Saxena K, Grimme S, Betz M, Schieborr U, Pescatore B, Langer T, Schwalbe H



PMID: 16034669 [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
Combinatorial triple-selective labeling as a tool to assist membrane protein backbone resonance assignment
Combinatorial triple-selective labeling as a tool to assist membrane protein backbone resonance assignment Abstract Obtaining NMR assignments for slowly tumbling molecules such as detergent-solubilized membrane proteins is often compromised by low sensitivity as well as spectral overlap. Both problems can be addressed by amino-acid specific isotope labeling in conjunction with 15Nâ??1H correlation experiments. In this work an extended combinatorial selective in vitro labeling scheme is proposed that seeks to reduce the number of samples required for assignment. Including three...
nmrlearner Journal club 0 01-21-2012 06:26 PM
RDC derived protein backbone resonance assignment using fragment assembly
RDC derived protein backbone resonance assignment using fragment assembly Abstract Experimental residual dipolar couplings (RDCs) in combination with structural models have the potential for accelerating the protein backbone resonance assignment process because RDCs can be measured accurately and interpreted quantitatively. However, this application has been limited due to the need for very high-resolution structural templates. Here, we introduce a new approach to resonance assignment based on optimal agreement between the experimental and calculated RDCs from a structural template that...
nmrlearner Journal club 0 12-31-2010 08:38 PM
[NMR paper] Reconsidering complete search algorithms for protein backbone NMR assignment.
Reconsidering complete search algorithms for protein backbone NMR assignment. Related Articles Reconsidering complete search algorithms for protein backbone NMR assignment. Bioinformatics. 2005 Sep 1;21 Suppl 2:ii230-6 Authors: Vitek O, Bailey-Kellogg C, Craig B, Kuliniewicz P, Vitek J MOTIVATION: Nuclear magnetic resonance (NMR) spectroscopy is widely used to determine and analyze protein structures. An essential step in NMR studies is determining the backbone resonance assignment, which maps individual atoms to experimentally measured...
nmrlearner Journal club 0 12-01-2010 06:56 PM
[NMR paper] NMR backbone assignment of a protein kinase catalytic domain by a combination of seve
NMR backbone assignment of a protein kinase catalytic domain by a combination of several approaches: application to the catalytic subunit of cAMP-dependent protein kinase. Related Articles NMR backbone assignment of a protein kinase catalytic domain by a combination of several approaches: application to the catalytic subunit of cAMP-dependent protein kinase. Chembiochem. 2004 Nov 5;5(11):1508-16 Authors: Langer T, Vogtherr M, Elshorst B, Betz M, Schieborr U, Saxena K, Schwalbe H Protein phosphorylation is one of the most important mechanisms...
nmrlearner Journal club 0 11-24-2010 10:03 PM
[NMR paper] Computational assignment of protein backbone NMR peaks by efficient bounding and filt
Computational assignment of protein backbone NMR peaks by efficient bounding and filtering. Related Articles Computational assignment of protein backbone NMR peaks by efficient bounding and filtering. J Bioinform Comput Biol. 2003 Jul;1(2):387-409 Authors: Lin G, Xu D, Chen ZZ, Jiang T, Wen J, Xu Y NMR resonance assignment is one of the key steps in solving an NMR protein structure. The assignment process links resonance peaks to individual residues of the target protein sequence, providing the prerequisite for establishing intra- and...
nmrlearner Journal club 0 11-24-2010 09:16 PM
[NMR paper] An efficient branch-and-bound algorithm for the assignment of protein backbone NMR pe
An efficient branch-and-bound algorithm for the assignment of protein backbone NMR peaks. Related Articles An efficient branch-and-bound algorithm for the assignment of protein backbone NMR peaks. Proc IEEE Comput Soc Bioinform Conf. 2002;1:165-74 Authors: Lin G, Xu D, Chen ZZ, Jiang T, Wen J, Xu Y NMR resonance assignment is one of the key steps in solving an NMR protein structure. The assignment process links resonance peaks to individual residues of the target protein sequence, providing the prerequisite for establishing intra- and...
nmrlearner Journal club 0 11-24-2010 08:49 PM
[NMR paper] A sequential HNCA NMR pulse sequence for protein backbone assignment.
A sequential HNCA NMR pulse sequence for protein backbone assignment. Related Articles A sequential HNCA NMR pulse sequence for protein backbone assignment. J Magn Reson. 2001 May;150(1):100-4 Authors: Meissner A, Sørensen OW The conventional HNCA pulse sequence suffers from the ambiguity that it cannot distinguish inter- and intraresidue correlations because the one-bond and two-bond J(NC(alpha)) coupling constants are of similar magnitude. This paper presents a novel pulse sequence, sequential HNCA, that leads to a spectrum exhibiting...
nmrlearner Journal club 0 11-19-2010 08:32 PM
[NMR paper] Activation of the phosphosignaling protein CheY. II. Analysis of activated mutants by
Activation of the phosphosignaling protein CheY. II. Analysis of activated mutants by 19F NMR and protein engineering. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc-MS.gif Related Articles Activation of the phosphosignaling protein CheY. II. Analysis of activated mutants by 19F NMR and protein engineering. J Biol Chem. 1993 Jun 25;268(18):13089-96 Authors: Bourret RB, Drake SK, Chervitz SA, Simon MI, Falke JJ The Escherichia coli CheY protein is activated by phosphorylation,...
nmrlearner Journal club 0 08-21-2010 11:53 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 08:14 AM.


Map