The amino acid acridon-2-ylalanine (Acd) can be a valuable probe of protein conformational change because it is a
long lifetime, visible wavelength fluorophore that is small enough to be incorporated during ribosomal biosynthesis. Incorporation
of Acd into proteins expressed in E. coli requires efficient chemical synthesis to produce large quantities...
The amino acid acridon-2-ylalanine (Acd) can be a valuable probe of protein conformational change because it is a
long lifetime, visible wavelength fluorophore that is small enough to be incorporated during ribosomal biosynthesis. Incorporation
of Acd into proteins expressed in E. coli requires efficient chemical synthesis to produce large quantities...
This project deals with a method to optimize in vivo labeling using small fluorescent molecules via bioorthogonal reactions. The reaction used involves our unnatural amino acid 4-(6-methyl-s-tetrazin-3-yl)aminophenylalanine (AMT-Phe). The amino acid is site-specifically incorporated into GFP and then reacted with a labeled, strained trans-cyclooctene, resulting in a labeled protein. However...
This project deals with a method to optimize in vivo labeling using small fluorescent molecules via bioorthogonal reactions. The reaction used involves our unnatural amino acid 4-(6-methyl-s-tetrazin-3-yl)aminophenylalanine (AMT-Phe). The amino acid is site-specifically incorporated into GFP and then reacted with a labeled, strained trans-cyclooctene, resulting in a labeled protein. However...
This project deals with a method to optimize in vivo labeling using small fluorescent molecules via bioorthogonal reactions. The reaction used involves our unnatural amino acid 4-(6-methyl-s-tetrazin-3-yl)aminophenylalanine (AMT-Phe). The amino acid is site-specifically incorporated into GFP and then reacted with a labeled, strained trans-cyclooctene, resulting in a labeled protein. However...
This project deals with a method to optimize in vivo labeling using small fluorescent molecules via bioorthogonal reactions. The reaction used involves our unnatural amino acid 4-(6-methyl-s-tetrazin-3-yl)aminophenylalanine (AMT-Phe). The amino acid is site-specifically incorporated into GFP and then reacted with a labeled, strained trans-cyclooctene, resulting in a labeled protein. However...
The interaction of lecithin-cholesterol acyltransferase (LCAT) with apolipoprotein A-I (apoA-I) plays a critical role in highdensity lipoprotein (HDL) maturation.Wepreviously identified a highly solvent-exposed apoA-I loop domain (Leu¹⁵⁹–Leu¹⁷⁰) in nascent HDL, the so-called “solar flare” (SF) region, and proposed that it serves as an LCAT docking site (Wu, Z., Wagner, M....
The amino acid acridon-2-ylalanine (Acd) can be a valuable probe of protein conformational change because it is a
long lifetime, visible wavelength fluorophore that is small enough to be incorporated during ribosomal biosynthesis. Incorporation
of Acd into proteins expressed in E. coli requires efficient chemical synthesis to produce large quantities...
The site-specific incorporation of non-canonical amino acids (ncAAs) into proteins is an important tool for understanding biological function. Traditionally, each new ncAA targeted requires a resource-consuming process of generating new ncAA aminoacyl tRNA synthetase/tRNACUA pairs. However, the discovery that some tRNA synthetases are “permissive,” in that they can incorporate multiple...
Stable surface adhesion of cells is one of the early pivotal steps in bacterial biofilm
formation, a prevalent adaptation strategy in response to changing environments. In Pseudomonas
fluorescens, this process is regulated by the Lap system and the second messenger cyclic-di-GMP.
High cytoplasmic levels of cyclic-di-GMP activate the transmembrane receptor...