In the present study, additional Trp-analogues and Trp-like amino acids containing sulphur (pharmacologically active substances), selenium (useful alternatives to SeMet for phase problem in X-ray crystallography), and amino group (the source of new spectral properties of 'gold' fluorescent protein) are chemically synthesised with the modified protocol and in vivo translated into proteins using selective pressure incorporation (SPI) method. The atomic structures of model ptotiens, human annexinV, barstar, and two variants of green fluorescent protein (EFGP, ECFP), containing these compounds were obtained using protein X-ray crystallography method.
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In the present study, additional Trp-analogues and Trp-like amino acids containing sulphur (pharmacologically active substances), selenium (useful alternatives to SeMet for phase problem in X-ray crystallography), and amino group (the source of new spectral properties of 'gold' fluorescent protein) are chemically synthesised with the modified protocol and in vivo translated into proteins using selective pressure incorporation (SPI) method. The atomic structures of model ptotiens, human annexinV,...
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