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Results: 4

1.
Figure 4

Figure 4. From: Proteins in Action: Femtosecond to Millisecond Structural Dynamics of a Photoactive Flavoprotein.

Transient IR spectra for dAppABLUF and two mutants. (A) Femtosecond to nanosecond TRIR of W104A. (B) Microsecond dynamics of W104A. (C) Comparison of the TRIR spectra of AppABLUF and the two mutants 10 ns after excitation. (D) As for (C) but 20 μs after excitation.

Richard Brust, et al. J Am Chem Soc. 2013 October 30;135(43):16168-16174.
2.
Figure 1

Figure 1. From: Proteins in Action: Femtosecond to Millisecond Structural Dynamics of a Photoactive Flavoprotein.

Structure and H-bonding of FAD in AppABLUF. (A) Crystal structure of AppABLUF showing flavin binding between helices 1 and 2. (B) The H-bonding network around the flavin that includes the key residues Y21, Q63, W104, and M106. The figure was made using Pymol,1 and the structure 1YRX.pdb.5 (C) Details of the proposed H-bonding network changes in dAppABLUF around the chromophore following photoexcitation.

Richard Brust, et al. J Am Chem Soc. 2013 October 30;135(43):16168-16174.
3.
Figure 3

Figure 3. From: Proteins in Action: Femtosecond to Millisecond Structural Dynamics of a Photoactive Flavoprotein.

Comparison of protein and chromophore mode kinetics. (A) Kinetics of protein modes, showing that the linked pair at 1622/1631 cm–1 exhibit distinct kinetics. The growth of the transient occurs more rapidly than the evolution of the bleach. (B) Kinetics associated with the recovery of the chromophore modes at 1547 cm–1 (complete recovery) and 1703 cm–1 (partial recovery (Figure 2B)) and the growth of the 1688 cm–1 transient. The slower dynamics associated with the chromophore recovery and growth of the light adapted state compared to the protein modes in (A) is apparent. The relevant optical density axes are indicated by the symbol color.

Richard Brust, et al. J Am Chem Soc. 2013 October 30;135(43):16168-16174.
4.
Figure 2

Figure 2. From: Proteins in Action: Femtosecond to Millisecond Structural Dynamics of a Photoactive Flavoprotein.

Time resolved IR difference spectra for dAppABLUF. (A) TRIR spectra recorded between 2 ps and 10 ns after excitation of dAppABLUF at 450 nm. The fast and complete decay of the singlet excited state is evident in the transient flavin modes at 1380 cm–1. However, the ground state recovery is incomplete, e.g., at 1547 cm–1 and some transient (probably triplet) state is formed. (B) Relaxation in the dAppABLUF TRIR spectrum between 10 ns and 50 μs after excitation. The electronic ground state recovers fully (1547 cm–1) but formation of a new environment is indicated by the shift and incomplete recovery in the carbonyl mode at 1703 cm–1. The temporal evolution in the 1622/1631 cm–1 pair of protein modes is also evident. .(C) Effect of 13C isotope exchange in dAppABLUF measured 10 ns and 20 μs after excitation. (D) Comparison of the TRIR spectra recorded 20 μs after excitation with the stationary state IR difference spectrum for the light minus dark states.

Richard Brust, et al. J Am Chem Soc. 2013 October 30;135(43):16168-16174.

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