Thioxylation as One-Atom-Substitution Generates a Photoswitchable Element within the Peptide Backbone

Frank, Robert; Jakob, Mario; Thunecke, Frank; Fischer, Gunter; Schutkowski, Mike

doi:10.1002/(sici)1521-3773(20000317)39:6<1120::aid-anie1120>3.3.co;2-8

Cited by 20 publications

(28 citation statements)

References 6 publications

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“…For example, the cis/trans prolyl peptide bond isomerization during collagen folding could be modulated by exploiting the tendency of thioamides to isomerize upon UV radiation. 24,50,51 In addition, thioamide-containing CMPs could be useful in high-throughput assays of collagen binding by accessing the ability of thioamides to quench pendant fluorophores. 52 Finally, thioamides are protease-resistant, 53 making thioamide-incorporation a potential strategy for producing robust collagen-based biomaterials.…”

mentioning

confidence: 99%

Thioamides in the collagen triple helix

2015

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mentioning

confidence: 99%

Thioamides in the collagen triple helix

2015

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“…Despite many successful applications of azobenzene-based cross-linkers, we note that developing reversible phototriggers is still a very active research area. For example, efforts to expand the excitation wavelength of azobenzene derivatives to the visible regime [86] and to identify/design other reversible phototriggers, such as spiropyrans [87] and thioamides [88-90], still continue.…”

Section: Triggering Protein Conformational Events With Lightmentioning

confidence: 99%

Tightening up the structure, lighting up the pathway: application of molecular constraints and light to manipulate protein folding, self-assembly and function

2014

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Chemical cross-linking provides an effective avenue to reduce the conformational entropy of polypeptide chains and hence has become a popular method to induce or force structural formation in peptides and proteins. Recently, other types of molecular constraints, especially photoresponsive linkers and functional groups, have also found increased use in a wide variety of applications. Herein, we provide a concise review of using various forms of molecular strategies to constrain proteins, thereby stabilizing their native states, gaining insight into their folding mechanisms, and/or providing a handle to trigger a conformational process of interest with light. The applications discussed here cover a wide range of topics, ranging from delineating the details of the protein folding energy landscape to controlling protein assembly and function.

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“…This wavelength is easily accessible for femtosecond lasers (since it is obtained by tripling the Ti:S laser wavelength), and S-O substitution may be done site-selectively. Furthermore, it has been shown that incorporation of a thioamide linkage results in only minor changes of the secondary structure of a peptide [83,84] and that secondary structure is indeed changing upon illumination of thiopeptides [85,86]. A recent combined theoretical-experimental femtosecond studies on the photoswitch itself (CH 3 -CSNH-CH 3 ) shows that the isomerization quantum yield is high (30-40%), that the molecule is stable against photodegeneration, and that the isomerization proceeds through two reaction channels, one ultrafast with a <5 ps time constant and one slower with a 200 ps time constant [87].…”

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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Thioxylation as One-Atom-Substitution Generates a Photoswitchable Element within the Peptide Backbone

Cited by 20 publications

References 6 publications

Thioamides in the collagen triple helix

Thioamides in the collagen triple helix

Tightening up the structure, lighting up the pathway: application of molecular constraints and light to manipulate protein folding, self-assembly and function

Ultrafast Peptide and Protein Dynamics by Vibrational Spectroscopy

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