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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 Improving Sensitivity of Solid-state NMR Spectroscopy by Rational Design of Polarizing Agents for Dynamic Nuclear Polarization #DNPNMR
From The DNP-NMR Blog: Improving Sensitivity of Solid-state NMR Spectroscopy by Rational Design of Polarizing Agents for Dynamic Nuclear Polarization #DNPNMR Kubicki, D.J. and L. Emsley, Improving Sensitivity of Solid-state NMR Spectroscopy by Rational Design of Polarizing Agents for Dynamic Nuclear Polarization. Chimia (Aarau), 2017. 71(4): p. 190-194. https://www.ncbi.nlm.nih.gov/pubmed/28446334
nmrlearner
Yesterday 06:16 PM
by nmrlearner Go to last post
0 6 News from NMR blogs
Go to first new post What will happen if we don't nurture the next generation of scientists? - The Globe and Mail
http://www.bionmr.com//t0.gstatic.com/images?q=tbn:ANd9GcRrxtw5_SNdaucYvTbBfkZ15e0BFX6gb9B4Oqio6ojmWohMqJnbDhB7Kwy6Fif297q7DZMjo-2r The Globe and Mail <img alt="" height="1" width="1"> What will happen if we don't nurture the next generation of scientists? The Globe and Mail I have spent my career developing nuclear magnetic resonance spectroscopy to study biological molecules. I have used this technology to study the properties of proteins, to see how they change their shapes and move in ways that influence the things ... What will happen if we don't nurture the next generation...
nmrlearner
Yesterday 06:16 PM
by nmrlearner Go to last post
0 11 Online News
Go to first new post [NMR paper] Cost-effective large-scale expression of proteins for NMR studies.
Cost-effective large-scale expression of proteins for NMR studies. Related Articles Cost-effective large-scale expression of proteins for NMR studies. J Biomol NMR. 2018 May 19;: Authors: Klopp J, Winterhalter A, Gbleux R, Scherer-Becker D, Ostermeier C, Gossert AD Abstract We present protocols for high-level expression of isotope-labelled proteins in E. coli in cost-effective ways. This includes production of large amounts of unlabeled proteins and 13C-methyl methionine labeling in rich media, where yields of up to a gram of...
nmrlearner
Yesterday 06:16 PM
by nmrlearner Go to last post
0 12 Journal club
Go to first new post Rapid measurement of long-range distances in proteins by multidimensional 13 C?? 19 F REDOR NMR under fast magic-angle spinning
Rapid measurement of long-range distances in proteins by multidimensional 13 C?? 19 F REDOR NMR under fast magic-angle spinning Abstract The ability to simultaneously measure many long-range distances is critical to efficient and accurate determination of protein structures by solid-state NMR (SSNMR). So far, the most common distance constraints for proteins are 13C??15N distances, which are usually measured using the rotational-echo double-resonance (REDOR) technique. However, these measurements are restricted to distances of up to ~??5*? due to...
nmrlearner
Yesterday 06:16 PM
by nmrlearner Go to last post
0 10 Journal club
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