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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 4 of 4
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Go to first new post Protein Crystallization Market to Observe Strong Development by 2020 - Medgadget (blog)
Protein Crystallization Market to Observe Strong Development by 2020 - Medgadget (blog) http://www.bionmr.com//t2.gstatic.com/images?q=tbn:ANd9GcT8odg9QMVMgeM_9WXyrMAR0ZnrBA5OsA2xy1L7maIXL5n-4TCmk4AUNwZNUWJiY4SnN-qwtF4 Medgadget (blog) <img alt="" height="1" width="1"> Protein Crystallization Market to Observe Strong Development by 2020 Medgadget (blog) Various techniques used during protein crystallization technology are ion-exchange chromatography, high-performance liquid chromatography (HPLC), gel-electrophoresis, x-ray crystallography and nuclear magnetic resonance (NMR). On the...
nmrlearner
Today 08:51 PM
by nmrlearner Go to last post
0 1 Online News
Go to first new post [NMR paper] Probing Medin Monomer Structure and its Amyloid Nucleation Using (13)C-Direct Detection NMR in Combination with Structural Bioinformatics.
Probing Medin Monomer Structure and its Amyloid Nucleation Using (13)C-Direct Detection NMR in Combination with Structural Bioinformatics. http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.nature.com-images-lo_npg.gif Related Articles Probing Medin Monomer Structure and its Amyloid Nucleation Using (13)C-Direct Detection NMR in Combination with Structural Bioinformatics. Sci Rep. 2017 Mar 22;7:45224 Authors: Davies HA, Rigden DJ, Phelan MM, Madine J Abstract Aortic medial amyloid is the most prevalent...
nmrlearner
Today 08:51 PM
by nmrlearner Go to last post
0 1 Journal club
Go to first new post [NMR paper] Cu(II)-Based Paramagnetic Probe to Study RNA-Protein Interactions by NMR.
Cu(II)-Based Paramagnetic Probe to Study RNA-Protein Interactions by NMR. Related Articles Cu(II)-Based Paramagnetic Probe to Study RNA-Protein Interactions by NMR. Inorg Chem. 2017 Mar 22; Authors: Seebald LM, DeMott CM, Ranganathan S, Asare Okai PN, Glazunova A, Chen A, Shekhtman A, Royzen M Abstract Paramagnetic NMR techniques allow for studying three-dimensional structures of RNA-protein complexes. In particular, paramagnetic relaxation enhancement (PRE) data can provide valuable information about long-range distances between...
nmrlearner
Today 08:51 PM
by nmrlearner Go to last post
0 1 Journal club
Go to first new post Interpolating and extrapolating with hmsIST:*seeking a t max for optimal sensitivity, resolution and frequency accuracy
Interpolating and extrapolating with hmsIST:*seeking a t max for optimal sensitivity, resolution and frequency accuracy Abstract Non-Uniform Sampling has the potential to exploit the optimal resolution of high-field NMR instruments. This is not possible in 3D and 4D NMR experiments when using traditional uniform sampling due to the long overall measurement time. Nominally, uniformly sampled time domain data acquired to a maximum evolution time tmax can be extended to high resolution via a virtual maximum evolution time t*max while extrapolating...
nmrlearner
Today 08:30 AM
by nmrlearner Go to last post
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