Tryptophan phosphorescence spectroscopy reveals that a domain in the NAD(H)-binding component (dI) of transhydrogenase from Rhodospirillum rubrum has an extremely rigid and conformationally homogeneous protein core.
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The role of invariant amino acid residues at the hydride transfer site of proton-translocating transhydrogenaseCavity-creating mutations in Pseudomonas aeruginosa azurin: effects on protein dynamics and stability.Mutations in transhydrogenase change the fluorescence emission state of TRP72 from 1La to 1Lb.Substrate-induced conformational changes in the membrane-embedded IIC(mtl)-domain of the mannitol permease from Escherichia coli, EnzymeII(mtl), probed by tryptophan phosphorescence spectroscopy.Substitution of tyrosine 146 in the dI component of proton-translocating transhydrogenase leads to reversible dissociation of the active dimer into inactive monomers.Isolation of Escherichia coli mannitol permease, EIImtl, trapped in amphipol A8-35 and fluorescein-labeled A8-35.
P2860
Tryptophan phosphorescence spectroscopy reveals that a domain in the NAD(H)-binding component (dI) of transhydrogenase from Rhodospirillum rubrum has an extremely rigid and conformationally homogeneous protein core.
description
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Tryptophan phosphorescence spectroscopy reveals that a domain in the NAD
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Tryptophan phosphorescence spe ...... ally homogeneous protein core.
@en
type
label
Tryptophan phosphorescence spectroscopy reveals that a domain in the NAD
@nl
Tryptophan phosphorescence spe ...... ally homogeneous protein core.
@en
prefLabel
Tryptophan phosphorescence spectroscopy reveals that a domain in the NAD
@nl
Tryptophan phosphorescence spe ...... ally homogeneous protein core.
@en
P2093
P2860
P356
P1476
Tryptophan phosphorescence spe ...... ally homogeneous protein core.
@en
P2093
Edi Gabellieri
Gijs I van Boxel
Giovanni B Strambini
J Baz Jackson
Jaap Broos
P2860
P304
47578-47584
P356
10.1074/JBC.M309287200
P407
P577
2003-09-12T00:00:00Z