- Abstract:
-
The signaling state of the photoactive yellow protein (PYP) photoreceptor is transiently developed via isomerization of its blue-light-absorbing chromophore. The associated structural rearrangements have large amplitude but, due to its transient nature and chemical exchange reactions that complicate NMR detection, its accurate three-dimensional structure in solution has been elusive. Here we report on direct structural observation of the transient signaling state by combining double electron ...
Expand abstract - Publication status:
- Published
- Publisher copy:
- 10.1021/ja200617t
-
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- Journal:
- Journal of the American Chemical Society
- Volume:
- 133
- Issue:
- 24
- Pages:
- 9395-9404
- Publication date:
- 2011-06-05
- DOI:
- EISSN:
-
1520-5126
- ISSN:
-
0002-7863
- URN:
-
uuid:644fc217-4df3-41b3-9c07-1014668b8b54
- Source identifiers:
-
142246
- Local pid:
- pubs:142246
- Copyright date:
- 2011
Journal article
The short-lived signaling state of the photoactive yellow protein photoreceptor revealed by combined structural probes.
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