Di-Cysteine S,S-Tetrazine: A Potential Ultra-fast Photochemical Trigger to Explore the Early Events of Peptide/Protein Folding.
Matthew J TuckerMohannad AbdoJoel R CourterJianxin ChenAmos B SmithRobin M HochstrasserPublished in: Journal of photochemistry and photobiology. A, Chemistry (2012)
The tetrazine chromophore holds promise as an effective photochemical trigger to achieve structural release, directed at the determination of peptide/protein motions that occur early in the folding processes. The photochemistry of 3,6-di-cysteine-S,S-tetrazines was examined by femtosecond IR transient absorption spectroscopy. Excitation of the tetrazine chromophore by visible and near UV light in the end yields chemically inert, structurally unobtrusive photoproducts that are not expected to interfere with the conformational dynamics of peptides and proteins. Dicysteine S,S-tetrazine is suggested to undergo photocleavage via a photochemical pathway different than the parent molecule s-tetrazine, based on kinetic measurements that reveal a stepwise reaction pathway of photofragmentation, whereby the initial ring cleavage event occurs prior to the formation of the SCN groups.
Keyphrases
- single molecule
- molecular dynamics simulations
- living cells
- high resolution
- amino acid
- fluorescent probe
- protein protein
- binding protein
- gene expression
- escherichia coli
- machine learning
- single cell
- molecular dynamics
- solid phase extraction
- risk assessment
- cerebral ischemia
- dna binding
- human health
- molecularly imprinted
- deep learning
- tandem mass spectrometry
- quantum dots