Two-dimensional (2D) optical spectroscopy utilizing multiple ultrafast coherent laser pulses
in the infrared or UV-vis frequency range has been used to study protein structure and …

How fast can a protein possibly fold? This question has stimulated experimentalists to seek
fast folding proteins and to engineer them to fold even faster. Proteins folding at or near the …

Two-Dimensional Optical Spectroscopy discusses the principles and applications of newly
emerging two-dimensional vibrational and optical spectroscopy techniques. It provides a …

In situ and real-time characterization of protein secondary structures at interfaces is
important in biological and bioengineering sciences, yet remains technically challenging. In …

The C-terminal domain of T4 fibritin (foldon) is obligatory for the formation of the fibritin trimer
structure and can be used as an artificial trimerization domain. Its native structure consists of …

Protein Folding Kinetics-Biophysical Methods (2nd Edition) gives a deep insight into the
principles and concepts of the kinetic and structural resolution of fast chemical and …

Both turn sequence and interstrand hydrophobic side-chain–side-chain interaction have
been suggested to be important determinants of β-hairpin stability. However, their roles in …

Modern experimental kinetics of protein folding began in the early 1990s with the
introduction of nanosecond laser pulses to trigger the folding reaction, providing an almost …

This Minireview focuses on the hemithioindigo photoswitch and its use for the reversible
control of three‐dimensional peptide structure and related biological functions. Both the …

We determine the reversible folding-unfolding of the C-terminal (41–56) fragment of protein
G as a function of density and temperature using replica exchange molecular dynamics …