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NMR processing:

NMR assignment:

Backbone:

Side-chains:

UNIO ATNOS-Ascan

NOEs:

UNIO ATNOS-Candid

Structure from NMR restraints:

Ab initio:

UNIO ATNOS-Candid

Fragment-based:

BMRB CS-Rosetta

Rosetta-NMR (Robetta)

Template-based:

Refinement:

Structure from chemical shifts:

Fragment-based:

WeNMR CS-Rosetta

BMRB CS-Rosetta

Homology-based:

Torsion angles from chemical shifts:

Promega- Proline

Secondary structure from chemical shifts:

CSI (via RCI server)

MICS caps, β-turns

Flexibility from chemical shifts:

Interactions from chemical shifts:

Chemical shifts re-referencing:

UNIO Shiftinspector

NMR model quality:

NOEs, other restraints:

Chemical shifts:

RDCs:

Pseudocontact shifts:

Protein geomtery:

Resolution-by-Proxy

SAVES2 or SAVES4

Ramachandran Plot

Quality Control Check

NMR spectrum prediction:

Flexibility from structure:

Molecular dynamics:

Chemical shifts prediction:

From structure:

CH3shift- Methyl

ArShift- Aromatic

CheShift-2- Cα

From sequence:

Disordered proteins:

Format conversion & validation:

From NMR-STAR 3.1

Validate NMR-STAR 3.1

NMR sample preparation:

Protein disorder:

Protein solubility:

Isotope labeling:

Solid-state NMR:

Showing results 1 to 2 of 2 Search took 0.00 seconds. Search: Posts From Last Day
		Thread / Thread Starter	Last Post	Replies	Views	Forum
		[NMR paper] High-Efficiency Trifluoromethyl-Methionine Incorporation into Cyclophilin A by Cell-Free Synthesis for 19F NMR Studies High-Efficiency Trifluoromethyl-Methionine Incorporation into Cyclophilin A by Cell-Free Synthesis for 19F NMR Studies Fluorine-19 NMR spectroscopy has emerged as a powerful tool for studying protein structure, dynamics, and interactions. Of particular interest is the exploitation of trifluoromethyl (tfm) groups, given their high sensitivity and superior transverse relaxation properties, compared to single fluorine atoms. However, biosynthetic incorporation of tfm-bearing amino acids remains challenging due to cytotoxicity and incompatibility with natural tRNA synthetases. Here, we report... nmrlearner	Today 12:06 AM by nmrlearner	0	15	Journal club
		1H Nuclear Magnetic Resonance Spectroscopy-Based Methods for the Quantification of Proteins in Urine - ACS Publications 1H Nuclear Magnetic Resonance Spectroscopy-Based Methods for the Quantification of Proteins in Urine ACS Publications 1H Nuclear Magnetic Resonance Spectroscopy-Based Methods for the Quantification of Proteins in Urine - ACS Publications More... nmrlearner	Yesterday 12:00 PM by nmrlearner	0	49	Online News
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