Femtosecond visible and infrared analogues of multiple-pulse nuclear magnetic resonance
techniques provide novel snapshot probes into the structure and electronic and vibrational …

▪ Abstract This review describes how kinetic experiments using techniques with dramatically
improved time resolution have contributed to understanding mechanisms in protein folding …

We have measured the kinetics of the helix-coil transition for the synthetic 21-residue
peptide Ac-WAAAH+ (AAAR+ A) 3A-NH2 initiated by nanosecond laser temperature jumps …

Most proteins are denatured by heat treatment, and the process is usually irreversible.
However, some proteins, such as hyperthermophilic proteins are known to be stable even at …

The structure of the transition state for the rate-limiting step in the folding and association of
the homodimeric coiled-coil peptide GCN4-p1, was probed by mutational analysis. A series …

The initial phase of folding for many proteins is presumed to be the collapse of the
polypeptide chain from expanded to compact, but still denatured, conformations. Theory and …

Ultrafast, laser-induced pH jump with time-resolved photoacoustic detection has been used
to investigate the early protonation steps leading to the formation of the compact acid …

The time, temperature, and sequence dependences of helix formation kinetics of fully
atomistic peptide models in explicit solvent are described quantitatively by a diffusive search …

Publisher Summary This chapter focuses on the experimental thermodynamic and structural
characterization of the barriers in the folding of single-domain globular proteins. The chapter …

Photoactivatable caged protons have been used to trigger proton transfer reactions in
aqueous solutions of acetate, glutamate, and poly-L-glutamic acid, and the volumetric and …