Time-resolved microspectroscopy on a single crystal of bacteriorhodopsin reveals lattice-induced differences in the photocycle kinetics.
about
Conformational exchange in a membrane transport protein is altered in protein crystals.Mutations that stabilize the open state of the Erwinia chrisanthemi ligand-gated ion channel fail to change the conformation of the pore domain in crystalsSynergy within structural biology of single crystal optical spectroscopy and X-ray crystallography.Long-distance proton transfer with a break in the bacteriorhodopsin active site.Electron paramagnetic resonance study of structural changes in the O photointermediate of bacteriorhodopsinChasing the open-state structure of pentameric ligand-gated ion channels.
P2860
Time-resolved microspectroscopy on a single crystal of bacteriorhodopsin reveals lattice-induced differences in the photocycle kinetics.
description
2006 nî lūn-bûn
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2006年の論文
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@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
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@zh-mo
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@wuu
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2006年论文
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name
Time-resolved microspectroscop ...... es in the photocycle kinetics.
@en
type
label
Time-resolved microspectroscop ...... es in the photocycle kinetics.
@en
prefLabel
Time-resolved microspectroscop ...... es in the photocycle kinetics.
@en
P2860
P1433
P1476
Time-resolved microspectroscop ...... es in the photocycle kinetics.
@en
P2093
P2860
P304
P356
10.1529/BIOPHYSJ.106.083345
P407
P577
2006-05-26T00:00:00Z