Structural rearrangements of the two domains of Azotobacter vinelandii rhodanese upon sulfane sulfur release: essential molecular dynamics, 15N NMR relaxation and deuterium exchange on the uniformly labeled protein.
about
A conserved mechanism for sulfonucleotide reductionNMR dynamic studies suggest that allosteric activation regulates ligand binding in chicken liver bile acid-binding protein.The N-terminal rhodanese domain from Azotobacter vinelandii has a stable and folded structure independently of the C-terminal domain.
P2860
Structural rearrangements of the two domains of Azotobacter vinelandii rhodanese upon sulfane sulfur release: essential molecular dynamics, 15N NMR relaxation and deuterium exchange on the uniformly labeled protein.
description
2003 nî lūn-bûn
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2003年の論文
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2003年学术文章
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name
Structural rearrangements of t ...... the uniformly labeled protein.
@en
Structural rearrangements of t ...... the uniformly labeled protein.
@nl
type
label
Structural rearrangements of t ...... the uniformly labeled protein.
@en
Structural rearrangements of t ...... the uniformly labeled protein.
@nl
prefLabel
Structural rearrangements of t ...... the uniformly labeled protein.
@en
Structural rearrangements of t ...... the uniformly labeled protein.
@nl
P2093
P50
P1476
Structural rearrangements of t ...... the uniformly labeled protein.
@en
P2093
Daniel Oscar Cicero
Giuseppe Brancato
Maria Orsale
Maurizio Paci
Silvia Pagani
P304
P356
10.1016/J.IJBIOMAC.2003.08.010
P577
2003-12-01T00:00:00Z