The ability to selectively modify proteins at two or more defined locations opens new
avenues for manipulating, engineering, and studying living systems. As a chemical biology …

More than two decades ago a general method to genetically encode noncanonical or
unnatural amino acids (NAAs) with diverse physical, chemical, or biological properties in …

We show that formyl benzeno boronic acids (2FBBA) selectively react with N-terminal
cysteines to yield a boronated thiazolidine featuring a B–N bond. The reaction exhibits a …

Fluorescence spectroscopy is a powerful tool for probing complex biological processes. The
ubiquity of peptide–protein and protein–protein interactions in these processes has made …

Highlights•Single-molecule FRET can be applied inside live cells.•Optimal labeling,
internalization and imaging strategies are being developed.•smFRET detection has been …

We have demonstrated the proof-of-concept of a label-free fluorescence quantitative
detection platform based on gold nanoparticle (AuNP) enhancement intrinsic fluorescence …

The ability to site-specifically modify proteins at multiple sites in vivo will enable the study of
protein function in its native environment with unprecedented levels of detail. Here, we …

Since its first demonstration about twenty years ago, single-molecule fluorescence
resonance energy transfer (FRET) has undergone remarkable technical advances. In this …

Trimethylsilyl (TMS) groups present outstanding NMR probes of biological macromolecules
as they produce intense singlets in 1H NMR spectra near 0 ppm, where few other proton …

In enzyme engineering, the main targets for enhancing properties are enzyme activity,
stereoselective specificity, stability, substrate range, and the development of unique …