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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


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Old 08-21-2010, 11:16 PM
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Default Biophysical aspects of the integrated combination of cytostatic drugs with radiothera

Biophysical aspects of the integrated combination of cytostatic drugs with radiotherapy. Part 1: In vitro investigations on the kinetics of activated isophosphamide metabolites and the determination of selective properties of DNA-interstrand and DNA-protein crosslinking mechanisms using 31P-NMR spectroscopy.

Related Articles Biophysical aspects of the integrated combination of cytostatic drugs with radiotherapy. Part 1: In vitro investigations on the kinetics of activated isophosphamide metabolites and the determination of selective properties of DNA-interstrand and DNA-protein crosslinking mechanisms using 31P-NMR spectroscopy.

Strahlenther Onkol. 1991 Jul;167(7):427-33

Authors: Ulmer W

The pH dependence of the kinetics of the "activated" isophosphamide metabolites 4-hydroxy-isophosphamide, isoaldophosphamide and isophosphoramide mustard has been characterized with the help of 31P-NMR Fourier spectroscopy. The most outstanding feature is the pH-dependence of the decay kinetics of 4-hydroxy-isophosphamide and isoaldophosphamide yielding the alkylating moiety isophosphoramide mustard and acrolein. With the same spectroscopic technique the alkylation of biomolecules containing guanine (cGMP, GDP, GTP, synthetic oligodeoxynucleic acid serving as a surrogate of DNA) and proteins containing cysteine as receptor molecule have been analyzed. The kinetic data provide information on combining the measured substrates with radiotherapy to be presented in further communications.

PMID: 1858021 [PubMed - indexed for MEDLINE]



Source: PubMed
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