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 05-31-2014, 01:57 PM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 20,028
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 Reply to Jensen and Blackledge: Dual quantifications of intrinsically disordered proteins by NMR ensembles and molecular dynamics simulations.

Reply to Jensen and Blackledge: Dual quantifications of intrinsically disordered proteins by NMR ensembles and molecular dynamics simulations.

Related Articles Reply to Jensen and Blackledge: Dual quantifications of intrinsically disordered proteins by NMR ensembles and molecular dynamics simulations.

Proc Natl Acad Sci U S A. 2014 Apr 22;111(16):E1559

Authors: Wang Y, Longhi S, Roche P, Wang J

PMID: 24877227 [PubMed - in process]



More...
Reply With Quote


Did you find this post helpful? Yes | No

Reply
Similar Threads
Thread Thread Starter Forum Replies Last Post
[NMR paper] NMR contributions to structural dynamics studies of intrinsically disordered proteins.
NMR contributions to structural dynamics studies of intrinsically disordered proteins. Related Articles NMR contributions to structural dynamics studies of intrinsically disordered proteins. J Magn Reson. 2014 Apr;241:74-85 Authors: Konrat R Abstract Intrinsically disordered proteins (IDPs) are characterized by substantial conformational plasticity. Given their inherent structural flexibility X-ray crystallography is not applicable to study these proteins. In contrast, NMR spectroscopy offers unique opportunities for structural and dynamic...
nmrlearner Journal club 0 03-25-2014 11:49 AM
[NMR paper] Toward optimal-resolution NMR of intrinsically disordered proteins.
Toward optimal-resolution NMR of intrinsically disordered proteins. Related Articles Toward optimal-resolution NMR of intrinsically disordered proteins. J Magn Reson. 2014 Apr;241:41-52 Authors: Nová?ek J, Zídek L, Sklená? V Abstract Proteins, which, in their native conditions, sample a multitude of distinct conformational states characterized by high spatiotemporal heterogeneity, most often termed as intrinsically disordered proteins (IDPs), have become a target of broad interest over the past 15years. With the growing evidence of their...
nmrlearner Journal club 0 03-25-2014 11:49 AM
Toward optimal-resolution NMR of intrinsically disordered proteins
Toward optimal-resolution NMR of intrinsically disordered proteins Publication date: April 2014 Source:Journal of Magnetic Resonance, Volume 241</br> Author(s): Ji?í Nová?ek , Lukáš Žídek , Vladimír Sklená?</br> Proteins, which, in their native conditions, sample a multitude of distinct conformational states characterized by high spatiotemporal heterogeneity, most often termed as intrinsically disordered proteins (IDPs), have become a target of broad interest over the past 15years. With the growing evidence of their important roles in fundamental cellular...
nmrlearner Journal club 0 03-21-2014 12:52 AM
NMR contributions to structural dynamics studies of intrinsically disordered proteins
NMR contributions to structural dynamics studies of intrinsically disordered proteins Publication date: April 2014 Source:Journal of Magnetic Resonance, Volume 241</br> Author(s): Robert Konrat</br> Intrinsically disordered proteins (IDPs) are characterized by substantial conformational plasticity. Given their inherent structural flexibility X-ray crystallography is not applicable to study these proteins. In contrast, NMR spectroscopy offers unique opportunities for structural and dynamic studies of IDPs. The past two decades have witnessed significant development...
nmrlearner Journal club 0 03-21-2014 12:52 AM
[NMR paper] Assessment of the Use of NMR Chemical Shifts as Replica-Averaged Structural Restraints in Molecular Dynamics Simulations to Characterize the Dynamics of Proteins.
Assessment of the Use of NMR Chemical Shifts as Replica-Averaged Structural Restraints in Molecular Dynamics Simulations to Characterize the Dynamics of Proteins. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Assessment of the Use of NMR Chemical Shifts as Replica-Averaged Structural Restraints in Molecular Dynamics Simulations to Characterize the Dynamics of Proteins. J Phys Chem B. 2013 Feb 1; Authors: Camilloni C, Cavalli A, Vendruscolo M Abstract It has been recently...
nmrlearner Journal club 0 02-03-2013 10:19 AM
From the Micelle to the Membrane: Molecular Dynamics Simulations of Solution NMR Structures of Membrane Proteins
From the Micelle to the Membrane: Molecular Dynamics Simulations of Solution NMR Structures of Membrane Proteins 29 January 2013 Publication year: 2013 Source:Biophysical Journal, Volume 104, Issue 2, Supplement 1</br> </br> </br> </br></br>
nmrlearner Journal club 0 02-03-2013 10:13 AM
Intrinsically disordered proteins - PhysicsToday.org
Intrinsically disordered proteins - PhysicsToday.org <img alt="" height="1" width="1" /> Intrinsically disordered proteins PhysicsToday.org Indeed, much of the community's understanding of protein function rests on our ability to deduce those structures by such methods as x-ray crystallography and nuclear magnetic resonance (NMR). The immense success and explanatory power of the ... Read here
nmrlearner Online News 0 08-01-2012 09:35 PM
Combining NMR ensembles and molecular dynamics simulations provides more realistic models of protein structures in solution and leads to better chemical shift prediction
Combining NMR ensembles and molecular dynamics simulations provides more realistic models of protein structures in solution and leads to better chemical shift prediction Abstract While chemical shifts are invaluable for obtaining structural information from proteins, they also offer one of the rare ways to obtain information about protein dynamics. A necessary tool in transforming chemical shifts into structural and dynamic information is chemical shift prediction. In our previous work we developed a method for 4D prediction of protein 1H chemical shifts in which molecular motions, the...
nmrlearner Journal club 0 02-11-2012 10:31 AM


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 - 2020, 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 05:50 PM.


Map