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


ABSTRACT: 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 ?360 picoseconds (ps) and ?9 nanoseconds (ns), which have not been clearly detected in previous studies.

SUBMITTER: Kim KH 

PROVIDER: S-EPMC2999690 | biostudies-literature | 2011 Jan

REPOSITORIES: biostudies-literature

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

Kim Kyung Hwan KH   Oang Key Young KY   Kim Jeongho J   Lee Jae Hyuk JH   Kim Youngmin Y   Ihee Hyotcherl H  

Chemical communications (Cambridge, England) 20100824 1


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 ∼360 picoseconds (ps) and ∼9 nanoseconds (ns), which have not been clearly detected in previous studies. ...[more]

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