The study of biomolecules in their native environments is a challenging task because of the
vast complexity of cellular systems. Technologies developed in the last few years for the …

Although chemists can synthesize virtually any small organic molecule, our ability to
rationally manipulate the structures of proteins is quite limited, despite their involvement in …

Proteins have evolved as a variable platform that provides access to molecules with diverse
shapes, sizes and functions. These features have inspired chemists for decades to seek …

In this paper, we present 1, 2, 3-triazole ε2-amino acids incorporated as a dipeptide
surrogate at three positions in the sequence of a known α-helical coiled coil. Biophysical …

Fluorescence resonance energy transfer and fluorescence polarization anisotropy are used
to investigate single molecules of the enzyme staphylococcal nuclease. Intramolecular …

Biomoleküle in ihrer natürlichen Umgebung zu erforschen, ist wegen der enormen
Komplexität zellulärer Systeme eine anspruchsvolle Aufgabe. In den letzten Jahren …

Nonsense suppression methodology, for incorporating unnatural amino acids into proteins,
has enabled a wide range of studies into protein structure and function using both in vitro …

Backbone hydrogen bonds (H-bonds) are prominent features of protein structures; however,
their role in protein folding remains controversial because they cannot be selectively …

An approach to identify backbone conformational changes underlying nicotinic acetylcholine
receptor (nAChR) gating was developed. Specific backbone peptide bonds were replaced …

The excised C-terminal thioesterase (TE) domain from the multidomain tyrocidine
nonribosomal peptide synthetase (NRPS) was recently shown to catalyze head-to-tail …