Infrared (IR) spectroscopy of the amide I band has been widely utilized for the analysis of
peptides and proteins. Theoretical modeling of IR spectra of proteins requires an accurate …

The aggregation of human amylin to form amyloid contributes to islet β-cell dysfunction in
type 2 diabetes. Studies of amyloid formation have been hindered by the low structural …

Two-dimensional infrared (2D IR) spectroscopy of mass-selected, cryogenically cooled
molecular ions is presented. Nonlinear response pathways, encoded in the time-domain …

Here, we present a new analysis program, AIM, that allows extracting the vibrational amide-I
Hamiltonian using molecular dynamics trajectories for protein infrared spectroscopy …

We provide a time-and structure-resolved characterization of the folding of the
heterogeneous β-hairpin peptide Tryptophan Zipper 2 (Trpzip2) using 2D IR spectroscopy …

Thioamides are sterically almost identical to their oxoamide counterparts, but they are
weaker hydrogen bond acceptors. Therefore, thioamide amino acids are excellent …

We proposed a computational protocol of simulating the T-jump peptide unfolding
experiments and the related transient IR and two-dimensional IR (2DIR) spectra based on …

Human islet amyloid polypeptide (hIAPP) aggregates into fibrils through oligomers that have
been postulated to contain α-helices as well as β-sheets. We employ a site-specific isotope …

We present a mixed quantum-classical model for studying the amide I vibrational dynamics
(predominantly CO stretching) in peptides and proteins containing proline. There are …

Intrinsically disordered proteins play an important role in biology, and unraveling their labile
structure presents a vital challenge. However, the dynamical structure of such proteins …