Time-resolved fluorescence spectroscopy is used to monitor molecular interactions and
motions that occur in the picosecond—nanosecond time range, and is especially useful in …

Discussions of biochemical fluorescence frequently start with the subject of protein
fluorescence. This is because, among biopolymers, proteins are unique in displaying useful …

Due to advances in methods for site-specific incorporation of unnatural amino acids (UAAs)
into proteins, a large number of UAAs with tailored chemical and/or physical properties have …

Fluorescence spectroscopy and its multiple applications to protein analysis, and to the life
sciences in general, have undergone rapid development during the past decade. This …

The biochemical flexibility of the cellular translation apparatus offers, in principle, a simple
route to the synthesis of drug-like modified peptides and novel biopolymers. However …

An orthogonal tryptophanyl–transfer RNA (tRNA) synthetase (TrpRS)-mutant opal
suppressor tRNATrp () pair was generated for use in mammalian cells. The anticodon loop …

7-Azaindole is the chromophoric moiety of 7-azatryptophan, which is an alternative to
tryptophan as an optical probe of protein structure and dynamics. The great power of the 7 …

Trans-4-hydroxyproline (Hyp) in eukaryotic proteins arises from post-translational
modification of proline residues. Because the modification enzyme is not present in …

Interaction of formononetin with a model transport protein, human serum albumin (HSA), has
been studied using fluorescence anisotropy, FT-IR spectroscopy, and molecular modeling …

The transcriptional activation domain of the herpesvirus protein VP16 resides in the carboxyl-
terminal 78 amino acids (residues 413-490). Fluorescence analyses of this domain …