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NMR processing:
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NMR assignment:
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MARS
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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
XPLOR-NIH
ASDP
UNIO ATNOS-Candid
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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)
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MICS caps, β-turns
d2D
PECAN
Flexibility from chemical shifts:
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Interactions from chemical shifts:
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Chemical shifts re-referencing:
Shiftcor
UNIO Shiftinspector
LACS
CheckShift
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V-NMR
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Methyl S2
B-factor
Molecular dynamics:
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From structure:
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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:
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Solid-state NMR:
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Default 13C magic angle spinning NMR evidence for a 15,15'-cis configuration of the spheroide

13C magic angle spinning NMR evidence for a 15,15'-cis configuration of the spheroidene in the Rhodobacter sphaeroides photosynthetic reaction center.

Related Articles 13C magic angle spinning NMR evidence for a 15,15'-cis configuration of the spheroidene in the Rhodobacter sphaeroides photosynthetic reaction center.

Biochemistry. 1992 Dec 15;31(49):12446-50

Authors: de Groot HJ, Gebhard R, van der Hoef I, Hoff AJ, Lugtenburg J, Violette CA, Frank HA

The photosynthetic reaction center of Rhodobacter sphaeroides 2.4.1 contains one carotenoid that protects the protein complex against photodestruction. The structure around the central (15,15') double bond of the bound spheroidene carotenoid was investigated with low-temperature magic angle spinning 13C NMR, which allows an in situ characterization of the configuration of the central double bond in the carotenoid. Carotenoidless reaction centers of R. sphaeroides R26 were reconstituted with spheroidene specifically labeled at the C-14' or C-15' position, and the signals from the labels were separated from the natural abundance background using 13C MAS NMR difference spectroscopy. The resonances shift 5.2 and 3.8 ppm upfield upon incorporation in the protein complex, similar to the 5.6 and 4.4 ppm upfield shift occurring in the model compound beta-carotene upon trans to 15,15'-cis isomerization. Hence the MAS NMR favors a cis configuration, as opposed to the trans configuration deduced from X-ray data.

PMID: 1463731 [PubMed - indexed for MEDLINE]



Source: PubMed
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