The kinetics of the helix⇌ coil transition of an alanine-based peptide following a laser-
induced temperature jump were monitored by the fluorescence of an N-terminal probe, 4 …

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 …

The helix-coil transition kinetics of an α-helical peptide were investigated by time-resolved
infrared spectroscopy coupled with laser-induced temperature-jump initiation method …

It is well-known that end caps and the peptide length can dramatically influence the
thermodynamics of the helix− coil transition. However, their roles in determining the kinetics …

Helices are ubiquitous in proteins. As such, the helix-coil transition has been studied
extensively. Seminal works1 of Schellman, Zimm and Bragg, Lifson and Roig, and Poland …

We report on the folding and unfolding dynamics of α-helix nucleation in two model helical
peptides. One of the peptides studied unfolds at lower temperatures (cold denatures) in …

We used UV resonance Raman spectroscopy to characterize the equilibrium conformation
and the kinetics of thermal denaturation of a 21 amino acid, mainly alanine, α-helical peptide …

Nanosecond laser temperature jumps and fluorescence detection were used to measure the
effect of viscosity on the kinetics of α-helix and β-hairpin formation in peptides containing 21 …

We study the reversible folding/unfolding of short Ala and Gly‐based peptides by molecular
dynamics simulations of all‐atom models in explicit water solvent. A kinetic analysis shows …

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 …