Publication: Long-Range conformational transition of a photoswitchable allosteric protein: Molecular dynamics simulation study
Long-Range conformational transition of a photoswitchable allosteric protein: Molecular dynamics simulation study
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Buchenberg, S., Knecht, V., Walser, R., Hamm, P., & Stock, G. (2014). Long-Range conformational transition of a photoswitchable allosteric protein: Molecular dynamics simulation study. Journal of Physical Chemistry B, 118, 13468–13476. https://doi.org/10.1021/jp506873y
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A local perturbation of a protein may lead to functional changes at some distal site. An example is the PDZ2 domain of human tyrosine phosphatase 1E which shows an allosteric transition upon binding to a peptide ligand. Recently Buchli et al. presented a time-resolved study of this transition by covalently linking an azobenzene photoswitch across the binding groove and using a femtosecond laser pulse that triggers the cis-trans photoisomerization of azobenzene. To aid the interpretation of these experiments, in this work seven microse
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Buchenberg, S., Knecht, V., Walser, R., Hamm, P., & Stock, G. (2014). Long-Range conformational transition of a photoswitchable allosteric protein: Molecular dynamics simulation study. Journal of Physical Chemistry B, 118, 13468–13476. https://doi.org/10.1021/jp506873y