Chemical dynamics in proteins: The photoisomerization of retinal in bacteriorhodopsin

Science

Volumn 279, Issue 5358, 1998, Pages 1886-1891

  Gai, Feng ^a,b   Hasson, K C ^a,c   McDonald, J Cooper ^a   Anfinrud, Philip A ^a  

^a HARVARD UNIVERSITY   (United States)

^b LOS ALAMOS NATIONAL LABORATORY   (United States)

^c Magnetic Imaging Technologies Inc   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIORHODOPSIN; RETINAL; SCHIFF BASE;

ABSORPTION SPECTROSCOPY; ARTICLE; ISOMERISM; MOLECULAR DYNAMICS; PHOTOREACTIVITY; PRIORITY JOURNAL;

BACTERIORHODOPSINS; HALOBACTERIUM SALINARUM; ISOMERISM; KINETICS; LIGHT; MODELS, CHEMICAL; PROTEIN CONFORMATION; RETINALDEHYDE; SPECTRUM ANALYSIS; THERMODYNAMICS;

EID: 0032549731     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.279.5358.1886     Document Type: Article

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75. Experimental methods: The pump pulse was generated by frequency doubling the signal output of a home-built β-barium borate - based optical parametric amplifier (OPA). The probe pulse was derived from a broadband continuum that was generated by focusing the output of a second OPA into a 3-mm sapphire crystal. A regeneratively amplified Ti:sapphire laser system (Clark-MXR, Dexter, MI) generated the optical pulses (1 kHz, 0.8 mJ, 120 fs, 780 nm) that powered the two OPAs. The bR sample (Sigma) was suspended in Hepes buffer (pH 7.4) and loaded into a sample cell with a 1-mm path length.
76. This work was supported in part by National Institutes of Health grant DK45306, the Beckman Foundation, the Mitsubishi Kasei Corporation, and the National Science Foundation (Young Investigator Award to P.A.A.; Graduate Research Fellowship to J.C.M.).