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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

Showing results 1 to 5 of 5
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Go to first new post [NMR paper] Applications of NMR to membrane proteins.
Applications of NMR to membrane proteins. Related Articles Applications of NMR to membrane proteins. Arch Biochem Biophys. 2017 May 18;: Authors: Opella SJ, Marassi FM Abstract Membrane proteins present a challenge for structural biology. In this article, we review some of the recent developments that advance the application of NMR to membrane proteins, with emphasis on structural studies in detergent-free, lipid bilayer samples that resemble the native environment. NMR spectroscopy is not only ideally suited for structure...
nmrlearner
Yesterday 04:45 PM
by nmrlearner Go to last post
0 3 Journal club
Go to first new post [NMR paper] Probing the Binding Modes of a Multi-Domain Protein to Lipid-Based Nanoparticles by Relaxation-Based NMR.
Probing the Binding Modes of a Multi-Domain Protein to Lipid-Based Nanoparticles by Relaxation-Based NMR. Related Articles Probing the Binding Modes of a Multi-Domain Protein to Lipid-Based Nanoparticles by Relaxation-Based NMR. J Phys Chem Lett. 2017 May 22;: Authors: Ceccon A, Tugarinov V, Boughton AJ, Fushman D, Clore GM Abstract The interactions of two model multi-domain proteins - covalently linked di-ubiquitins, Ub2 - with lipid-based nanoparticles have been quantitatively probed by the measurements of NMR lifetime...
nmrlearner
Yesterday 04:45 PM
by nmrlearner Go to last post
0 3 Journal club
Go to first new post NMR Analysis of Amide Hydrogen Exchange Rates in a Pentapeptide-Repeat Protein from A.*thaliana
NMR Analysis of Amide Hydrogen Exchange Rates in a Pentapeptide-Repeat Protein from A.*thaliana Publication date: 23 May 2017 Source:Biophysical Journal, Volume 112, Issue 10</br> Author(s): Shenyuan Xu, Shuisong Ni, Michael A. Kennedy</br> At2g44920 from Arabidopsis thaliana is a pentapeptide-repeat protein (PRP) composed of 25 repeats capped by*N- and C-terminal ?-helices. PRP structures are dominated by four-sided right-handed ?-helices typically consisting of mixtures of type II and type IV ?-turns. PRPs adopt repeated five-residue (Rfr) folds with an Rfr...
nmrlearner
Yesterday 04:45 PM
by nmrlearner Go to last post
0 2 Journal club
Go to first new post Molecular dynamics-based selectivity for Fast-Field-Cycling relaxometry by Overhauser and solid effect dynamic nuclear polarization #DNPNMR
From The DNP-NMR Blog: Molecular dynamics-based selectivity for Fast-Field-Cycling relaxometry by Overhauser and solid effect dynamic nuclear polarization #DNPNMR p.p1 {margin: 0.0px 0.0px 0.0px 36.0px; text-indent: -36.0px; font: 12.0px Helvetica} Neudert, O., C. Mattea, and S. Stapf, Molecular dynamics-based selectivity for Fast-Field-Cycling relaxometry by Overhauser and solid effect dynamic nuclear polarization. J. Magn. Reson., 2017. 276: p. 113-121. http://www.sciencedirect.com/science/article/pii/S1090780717300204
nmrlearner
Yesterday 04:44 AM
by nmrlearner Go to last post
0 3 News from NMR blogs
Go to first new post Conformational dynamics and alignment properties of loop lanthanide-binding-tags (LBTs) studied in interleukin-1β
Conformational dynamics and alignment properties of loop lanthanide-binding-tags (LBTs) studied in interleukin-1β Abstract Encodable lanthanide binding tags (LBTs) have become an attractive tool in modern structural biology as they can be expressed as fusion proteins of targets of choice. Previously, we have demonstrated the feasibility of inserting encodable LBTs into loop positions of interleukin-1β (Barthelmes et al. in J Am Chem Soc 133:808??819, 2011). Here, we investigate the differences in fast dynamics of selected loop-LBT interleukin-1β...
nmrlearner
Yesterday 04:44 AM
by nmrlearner Go to last post
0 16 Journal club
Showing results 1 to 5 of 5

 
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