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Webservers
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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
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Probing Microenvironmental Acidity in Lyophilized Protein and Vaccine Formulations Using Solid-state NMR ... - ScienceDirect.com
Probing Microenvironmental Acidity in Lyophilized Protein and Vaccine Formulations Using Solid-state NMR ... - ScienceDirect.com Probing Microenvironmental Acidity in Lyophilized Protein and Vaccine Formulations Using Solid-state NMR ... ScienceDirect.com Read here
nmrlearner
Yesterday
08:41 PM
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nmrlearner
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Online News
[NMR paper]
Fluorinated tags to study protein conformation and interactions using 19F NMR
Fluorinated tags to study protein conformation and interactions using 19F NMR The incorporation of fluorine atoms into a biomacromolecule provides a background-free and environmentally sensitive reporter of structure, conformation and interactions using 19F NMR. There are several methods to introduce the 19F reporter - either by synthetic incorporation via solid phase peptide synthesis; by suppressing the incorporation or biosynthesis of a natural amino acid and supplementing the growth media with a fluorinated counterpart during protein expression; and by genetic code... More...
nmrlearner
Yesterday
08:41 PM
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nmrlearner
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4
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[NMR paper]
A Hybrid Nanotube Stamp System in Intracellular Protein Delivery for Cancer Treatment and NMR Analytical Techniques
A Hybrid Nanotube Stamp System in Intracellular Protein Delivery for Cancer Treatment and NMR Analytical Techniques In contrast to intracellular gene transfer, the direct delivery of expressed proteins is a significantly challenging yet essential technique for elucidating cellular functions, including protein complex structure, liquid-liquid phase separation, therapeutic applications, and reprogramming. In this study, we developed a hybrid nanotube (HyNT) stamp system that physically inserts the HyNTs into adhesive cells, enabling the injection of target molecules through HyNT ducts. This...
nmrlearner
Yesterday
08:41 PM
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nmrlearner
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3
Journal club
[NMR paper]
Decoding the mechanism governing the structural stability of wheat germ agglutinin and its isolated domains: A combined calorimetric, NMR, and MD simulation study
Decoding the mechanism governing the structural stability of wheat germ agglutinin and its isolated domains: A combined calorimetric, NMR, and MD simulation study Wheat germ agglutinin (WGA) demonstrates potential as an oral delivery agent owing to its selective binding to carbohydrates and its capacity to traverse biological membranes. In this study, we employed differential scanning calorimetry and molecular dynamics simulations to comprehensively characterize the thermal unfolding process of both the complete lectin and its four isolated domains. Furthermore, we present the nuclear...
nmrlearner
Yesterday
08:41 PM
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nmrlearner
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[NMR paper]
Taylor Dispersion-Induced Phase Separation for the Efficient Characterisation of Protein Condensate Formation
Taylor Dispersion-Induced Phase Separation for the Efficient Characterisation of Protein Condensate Formation Angewandte Chemie International Edition, EarlyView. More...
nmrlearner
Yesterday
08:33 AM
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nmrlearner
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