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...
An ideal labeling reaction between protein and surface should generate a protein-patterned surface with control over the orientation of the desired protein. Controlling orientation would generate a homogeneous, un-fouled protein surface and allow for maximum efficiency in regards to the activity, reactivity, and stability of the protein. In this research...
Current protein immobilization techniques lack defined control over protein orientation. Protein orientation is important for making biosensors and biomaterials that are sensitive and efficient and can be crucial for designing some devices such as immunosensors or direct electron transferring biocells. A new method of protein immobilization is proposed that takes...
Current protein immobilization techniques lack defined control over protein orientation. Protein orientation is important for making biosensors and biomaterials that are sensitive and efficient and can be crucial for designing some devices such as immunosensors or direct electron transferring biocells. A new method of protein immobilization is proposed that takes...
A specific tyrosine post-translational modification, called 3-nitro-tyrosine (nitroTyr), has been known to be present on an essential calcium signaling protein called calmodulin (CaM) during oxidative stress. While protein-bound 3-nitro-tyrosine has long been considered a biomarker of OS, it is also hypothesized to be a mechanism for protein signaling. However, purification...
Genetic code expansion is a technology that allows for site-specific incorporation of noncanonical amino acids into recombinant proteins at amber stop codons using engineered translational machinery. The technology allows for expanded study into proteins, derived from the integration of novel chemical functions found in noncanonical amino acids, such as fluorescence,...