Proteins exhibit structural fluctuations over decades of time scales. From the picosecond
side chain motions to aggregates that form over the course of minutes, characterizing protein …

Infrared spectroscopy has played an instrumental role in the study of a wide variety of
biological questions. However, in many cases, it is impossible or difficult to rely on the …

Vibrational probes can provide a direct readout of the local electrostatic field in complex
molecular environments, such as protein binding sites and enzyme active sites. This …

Prediction of protein secondary structure from FTIR spectra usually relies on the absorbance
in the amide I–amide II region of the spectrum. It assumes that the absorbance in this …

The advent of laser-based sources of ultrafast infrared pulses has extended the study of very
fast molecular dynamics to the observation of processes manifested through their effects on …

Cells achieve high spatiotemporal control over biochemical processes through
compartmentalization to membrane-bound as well as membraneless organelles that …

In this study, we established an ultrasensitive electrochemical immunosensor based on the
gold nanoparticles-enhanced tyramide signal amplification (AuNPs-TSA) for the detection of …

Infrared spectroscopy is playing an important role in the elucidation of amyloid fiber
formation, but the coupling models that link spectra to structure are not well tested for …

Ultrafast two-dimensional infrared (2D IR) spectroscopy and Fourier transform infrared
(FTIR) spectroscopy are often performed in tandem, with FTIR typically used to interpret and …

Two-dimensional (2D) vibrational echo spectroscopy has previously been applied to
structural determination of small peptides. Here we extend the technique to a more complex …