A comparison between vertical winds and divergence in the high-latitude thermosphere

1993/08/01 by Nanxi Wang, Bing Yang, Caiyun Fu +11 · 28 citations
Biochemistry, Genetics and Molecular Biology · Chemistry · Earth and Planetary Sciences · Environmental Science · Medicine · #Altitude (triangle) #Amino acid #Atmospheric sciences #Biochemistry #Biology #Chemical Synthesis and Analysis #Chemical biology #Chemistry #Click Chemistry and Applications #Combinatorial chemistry #Covalent bond #Divergence (linguistics) #Enzyme #Genetics #Geodesy #Geology #Geomagnetism and Paleomagnetism Studies #Geometry #Geophysics #Geophysics and Gravity Measurements #Histidine #In vivo #Ionosphere #Latitude #Lysine #Meteorology #Methane Hydrates and Related Phenomena #Monoclonal and Polyclonal Antibodies Research #Organic chemistry #Physics #Protein engineering #Reactivity (psychology) #Thermosphere #Troposphere #Tyrosine

paper · open access · doi:10.1021/jacs.8b01087

published in Annales Geophysicae 11(8), 728-733 (Copernicus Publications)

openalex publication_date 1993/08/01 · openalex created_date 2016/06/24 · openalex updated_date 2026/08/01

Abstract

Introducing new chemical reactivity into proteins in living cells would endow innovative covalent bonding ability to proteins for research and engineering in vivo. Latent bioreactive unnatural amino acids (Uaas) can be incorporated into proteins to react with target natural amino acid residues via proximity-enabled reactivity. To expand the diversity of proteins amenable to such reactivity in vivo, a chemical functionality that is biocompatible and able to react with multiple natural residues under physiological conditions is highly desirable. Here we report the genetic encoding of fluorosulfate-l-tyrosine (FSY), the first latent bioreactive Uaa that undergoes sulfur-fluoride exchange (SuFEx) on proteins in vivo. FSY was found nontoxic to Escherichia coli and mammalian cells; after being incorporated into proteins, it selectively reacted with proximal lysine, histidine, and tyrosine via SuFEx, generating covalent intraprotein bridge and interprotein cross-link of interacting proteins directly in living cells. The proximity-activatable reactivity, multitargeting ability, and excellent biocompatibility of FSY will be invaluable for covalent manipulation of proteins in vivo. Moreover, genetically encoded FSY hereby empowers general proteins with the next generation of click chemistry, SuFEx, which will afford broad utilities in chemical biology, drug discovery, and biotherapeutics.

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