NMR analysis shows that a b-type variant of Hydrogenobacter thermophilus cytochrome c552 retains its native structure.
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The chemistry and biochemistry of heme c: functional bases for covalent attachmentDesign and fine-tuning redox potentials of metalloproteins involved in electron transfer in bioenergetics.Metalloproteins containing cytochrome, iron-sulfur, or copper redox centersComparison of the backbone dynamics of wild-type Hydrogenobacter thermophilus cytochrome c(552) and its b-type variant.In vitro studies on thioether bond formation between Hydrogenobacter thermophilus apocytochrome c(552) with metalloprotoporphyrin derivatives.
P2860
NMR analysis shows that a b-type variant of Hydrogenobacter thermophilus cytochrome c552 retains its native structure.
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NMR analysis shows that a b-ty ...... retains its native structure.
@en
NMR analysis shows that a b-ty ...... retains its native structure.
@nl
type
label
NMR analysis shows that a b-ty ...... retains its native structure.
@en
NMR analysis shows that a b-ty ...... retains its native structure.
@nl
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NMR analysis shows that a b-ty ...... retains its native structure.
@en
NMR analysis shows that a b-ty ...... retains its native structure.
@nl
P2093
P2860
P356
P1476
NMR analysis shows that a b-ty ...... retains its native structure.
@en
P2093
Lorna J Smith
Rachel Wain
Stuart J Ferguson
P2860
P304
15177-15182
P356
10.1074/JBC.M311869200
P407
P577
2004-01-15T00:00:00Z