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NMR processing:
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NMR assignment:
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PINE
Side-chains:
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NOEs:
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UNIO Candid
ASDP
Structure from NMR restraints:
Ab initio:
GeNMR
Cyana
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UNIO ATNOS-Candid
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Fragment-based:
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Template-based:
GeNMR
I-TASSER
Refinement:
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Structure from chemical shifts:
Fragment-based:
WeNMR CS-Rosetta
BMRB CS-Rosetta
Homology-based:
CS23D
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Torsion angles from chemical shifts:
Preditor
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Secondary structure from chemical shifts:
CSI (via RCI server)
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Flexibility from chemical shifts:
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Interactions from chemical shifts:
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Chemical shifts re-referencing:
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UNIO Shiftinspector
LACS
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NMR model quality:
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iCing
RDCs:
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Pseudocontact shifts:
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Protein geomtery:
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What-If
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SAVES2 or SAVES4
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NMR spectrum prediction:
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V-NMR
Flexibility from structure:
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Methyl S2
B-factor
Molecular dynamics:
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Chemical shifts prediction:
From structure:
Shiftx2
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CH3shift- Methyl
ArShift- Aromatic
ShiftS
Proshift
PPM
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From sequence:
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Poulsen_rc_CS
Disordered proteins:
MAXOCC
Format conversion & validation:
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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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Default Investigation of oxidation state-dependent conformational changes in Desulfovibrio vu

Investigation of oxidation state-dependent conformational changes in Desulfovibrio vulgaris Hildenborough cytochrome c553 by two-dimensional H-NMR spectra.

Related Articles Investigation of oxidation state-dependent conformational changes in Desulfovibrio vulgaris Hildenborough cytochrome c553 by two-dimensional H-NMR spectra.

FEBS Lett. 1996 Jul 1;389(2):203-9

Authors: Blanchard L, Blackledge MJ, Marion D, Guerlesquin F

Two-dimensional nuclear magnetic resonance spectroscopy (2D-NMR) was used to assign the proton resonances of ferricytochrome C553 from Desulfovibrio vulgaris Hildenborough. The spin systems of 76 out of 79 amino acids were identified by J-correlation spectroscopy (COSY and HOHAHA) in H20 and D20 and correlated by nuclear Overhauser effect spectroscopy (NOESY). The proton chemical shifts are compared in both oxidized and reduced states of the protein at 23 degrees C and pH 5.9. Chemical shift variations between reduced and oxidized states are due to the paramagnetic contribution. Medium and long-range nOe demonstrate the lack of major changes between the two redox states. NMR data provide evidence that in this low oxidoreduction potential cytochrome, the oxidized state is more rigid than the reduced state.

PMID: 8766830 [PubMed - indexed for MEDLINE]



Source: PubMed
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