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NMR processing:
MDD
NMR assignment:
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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:
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Vasco
iCing
RDCs:
DC
Anisofit
Pseudocontact shifts:
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Protein geomtery:
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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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Old 08-22-2010, 02:27 PM
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Default In vitro NMR proton T1 measurements in peritoneal ascites.

In vitro NMR proton T1 measurements in peritoneal ascites.

Related Articles In vitro NMR proton T1 measurements in peritoneal ascites.

Phys Med Biol. 1996 Mar;41(3):539-49

Authors: Yilmaz A, Tez M, Göral V, Boylu S, Kaplan A, Kavak G

The proton spin-lattice relaxation rate (1/T1) in malignant and non-malignant ascites was measured with an FT NMR spectrometer operating at 60 MHz. The mean relaxation rate in non-malignant ascites was significantly smaller than that of malignant ascites. However, the 1/T1 of malignant ascites overlaps with that of non-malignant ascites over all concentrations of total protein (TP) in samples. The 1/T1 in non-malignant ascites correlates strongly with TP, whilst the 1/T1 in malignant ascites shows only a moderate correlation. T1 measurements before and after addition of ascorbic acid (reductant) suggest that there is a small paramagnetic contribution of ions to the 1/T1 in malignant ascites. The least-squares fitting of 1/T1 versus TP for non-malignant data gives a linear relationship, and suggests that the T1 mechanism in non-malignant ascites is caused by a fast chemical exchange of water molecules between protein-bound water and free water.

PMID: 8778831 [PubMed - indexed for MEDLINE]



Source: PubMed
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