Direct observation of myoglobin structural dynamics from 100 picoseconds to 1 microsecond with picosecond X-ray solution scattering

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Here we report structural dynamics of equine myoglobin (Mb) in response to the CO photodissociation visualized by picosecond time-resolved X-ray solution scattering. The data clearly reveal new structural dynamics that occur in the timescale of similar to 360 picoseconds (ps) and similar to 9 nanoseconds (ns), which have not been clearly detected in previous studies.
Publisher
ROYAL SOC CHEMISTRY
Issue Date
2011
Language
English
Article Type
Article
Keywords

CARBON-MONOXIDE; CIRCULAR-DICHROISM; PROTEIN DYNAMICS; LIGAND-BINDING; CRYSTALLOGRAPHY; PHOTODISSOCIATION; SPECTROSCOPY; HEMOGLOBIN; ABSORPTION; COMPLEX

Citation

CHEMICAL COMMUNICATIONS, v.47, no.1, pp.289 - 291

ISSN
1359-7345
DOI
10.1039/c0cc01817a
URI
http://hdl.handle.net/10203/251061
Appears in Collection
CH-Journal Papers(저널논문)
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