Aminothiotyrosine Disulfide, an Optical Trigger for Initiation of Protein Folding

Lu, Helen S. M.; Völk, Martin; Kholodenko, Yuriy; Gooding, E.; Hochstrasser, Robin M.; DeGrado, William F.

doi:10.1021/ja970567o

Cited by 88 publications

(105 citation statements)

References 44 publications

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“…Upon photocleavage of the disulfide bridge, the hydrogen bond in the β-turn is destabilized and the ring structure opens. In contrast to the molecule studied by Hochstrasser and coworkers (131,132), this molecule is much more strained owing to the shortness of the backbone and stays open on long timescales. In fact, only approximately half the radicals are quenched after 1 ms either intra-or intermolecularily (134).…”

Section: Intrinsic Photoswitchesmentioning

confidence: 84%

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Two-Dimensional Infrared Spectroscopy of Photoswitchable Peptides

Hamm

Helbing

Bredenbeck

2008

Annu. Rev. Phys. Chem.

165

150

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We present a detailed discussion of the complimentary fields of the application of two-dimensional infrared (2D-IR) spectroscopy in comparison with two-dimensional nuclear magnetic resonance (2D-NMR) spectroscopy. Transient 2D-IR (T2D-IR) spectroscopy of nonequilibrium ensembles is probably one of the most promising strengths of 2D-IR spectroscopy, as the possibilities of 2D-NMR spectroscopy are limited in this regime. T2D-IR spectroscopy uniquely combines ultrafast time resolution with microscopic structural resolution. In this article we summarize our recent efforts to investigate the ultrafast structural dynamics of small peptides, such as the unfolding of peptide secondary structure motifs. The work requires two ingredients: 2D-IR spectroscopy and the possibility of triggering a structural transition of a peptide on an ultrafast timescale using embedded or intrinsic photoswitches. Several photoswitches have been tested, and we discuss our progress in merging these two pathways of research. AbstractWe present a detailed discussion of the complimentary fields of the application of two-dimensional infrared (2D-IR) spectroscopy in comparison with two-dimensional nuclear magnetic resonance (2D-NMR) spectroscopy. Transient 2D-IR (T2D-IR) spectroscopy of nonequilibrium ensembles is probably one of the most promising strengths of 2D-IR spectroscopy, as the possibilities of 2D-NMR spectroscopy are limited in this regime. T2D-IR spectroscopy uniquely combines ultrafast time resolution with microscopic structural resolution. In this article we summarize our recent efforts to investigate the ultrafast structural dynamics of small peptides, such as the unfolding of peptide secondary structure motifs. The work requires two ingredients: 2D-IR spectroscopy and the possibility of triggering a structural transition of a peptide on an ultrafast timescale using embedded or intrinsic photoswitches. Several photoswitches have been tested, and we discuss our progress in merging these two pathways of research.

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Section: Intrinsic Photoswitchesmentioning

confidence: 84%

“…Hochstrasser and coworkers (131,132) first reported this concept in their pioneering work. A 20-residue peptide was designed to fold into an α-helix after photocleavage, while no distinct secondary structure was possible in the initial bridged state.…”

Section: Intrinsic Photoswitchesmentioning

confidence: 99%

Two-Dimensional Infrared Spectroscopy of Photoswitchable Peptides

Hamm

Helbing

Bredenbeck

2008

Annu. Rev. Phys. Chem.

165

150

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“…The higher order of multi-photon absorption present in the measurement depends on the wavelength of light and the energy levels of the sample (Selvan et al, 2002). The normalized change in transmitted intensity can be approximated by the following equation (Hutchings, SheikBahae, Hagan, & Van Stryland, 1992;Lu et al, 1997;Van Stryland & Sheik-Bahae, 1998;Selvan et al, 2002):…”

Section: Open Aperture Z-scanmentioning

confidence: 99%

Studying the Linear and Nonlinear Optical Properties by Using Z-Scan Technique for CdS Thin Films Prepared by CBD Technique

Jabbar¹,

Abbas²,

Alzubaidy³

2018

APR

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CdS films prepared by using CBD technique, linear optical properties tests measured by UV-3000 Nano from OPTIMA, nonlinear properties contained the nonlinear refractive index and nonlinear absorption coefficient by using single light beam source green semiconductor developed laser (SZ-303 LASER) with material Nd:YVO4+KTP or Aluminum Alloy, and Wavelength Range is (532 nm), Beam Dimension 6 Meter distance Output Laser spot 18 mm ± 2.0 mm.

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“…• Photo-cleavable disulfide-bridges: The first approach in this direction was undertaken by Hochstrasser and coworkers in pioneering work, who optically dissociated a disulfide-bridge between two amino acids in a short peptide by exciting it with a short UV pulse at 270 nm [101,102]. The peptide was designed to fold into an α-helix after photo-cleavage, while no distinct secondary structure was possible in the initial bridged state.…”

Section: Vibrational Spectroscopy Of Non-equilibrium Dynamics Of Peptmentioning

confidence: 99%

Ultrafast Peptide and Protein Dynamics by Vibrational Spectroscopy

Hamm

2008

Biological and Medical Physics, Biomedical Engineering

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Ultrafast peptide and protein dynamics by vibrational spectroscopyHamm, P Hamm, P (2008). Ultrafast peptide and protein dynamics by vibrational spectroscopy. In: Braun, M; Gilch, P; Zinth, W. Ultrashort laser pulses in biology and medicine. Proteins are molecular machines with a well-defined 3D structure, and it is mainly the success of X-ray and NMR spectroscopic techniques that made the tremendous progress in structural biology happen. However, it is also clear that biomolecular processes generally involve conformational changes of proteins and enzymes. Mostly due to a lack of appropriate spectroscopic tools, much less is known about the dynamics of protein structures. Protein dynamics occurs on a large range of time scales, which can coarsely be related to various length scales: Dynamics of tertiary and quaternary structure extends from milliseconds to seconds and even longer, while formation of secondary structure has been observed between 50 ns and a few microseconds [1][2][3][4][5][6][7][8][9][10][11][12]. Nevertheless, several experiments have provided strong hints for the relevance of even faster processes from the observation of large instantaneous signals, which could not be time-resolved [2,7,13]. For example, Thompson et al.[5] estimated a "zipping time" for a 21-residue α-helix of 300 ps (i.e., the time for closing of subsequent hydrogen bonds, once an initial helix turn is formed), while Huang et al. [7] indirectly concluded that helix nucleation might occur on a subnanosecond time scale. Also molecular dynamics (MD) simulations suggest that peptides and proteins can undergo considerable structural changes within 1 ns or less [8-10, 14, 15]. Hummer et al. [16] found the formation of the first α-helical turn within 0.1-1 ns in work on helix nucleation in short Ala and Gly based peptides. Daura et al. [9,17] simulated equilibrium folding/unfolding of a β-heptapeptide at the melting point and above to obtain statistics on the populations of the folded and unfolded states. Several folding/unfolding events were observed in a 50 ns trajectory, where the actual transitions from unfolded to folded conformations could be as fast as 50-100ps.

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Aminothiotyrosine Disulfide, an Optical Trigger for Initiation of Protein Folding

Cited by 88 publications

References 44 publications

Two-Dimensional Infrared Spectroscopy of Photoswitchable Peptides

Two-Dimensional Infrared Spectroscopy of Photoswitchable Peptides

Studying the Linear and Nonlinear Optical Properties by Using Z-Scan Technique for CdS Thin Films Prepared by CBD Technique

Ultrafast Peptide and Protein Dynamics by Vibrational Spectroscopy

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