2017
DOI: 10.1039/c6cp08924k
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Microscopic nucleation and propagation rates of an alanine-based α-helix

Abstract: An infrared temperature-jump (T-jump) study by Huang et al. (Proc. Natl. Acad. Sci. 2002 99, 2788–2793) showed that the conformational relaxation kinetics of an alanine-based α-helical peptide depend not only on the final temperature (Tf) but also on the initial temperature (Ti) when Tf is fixed. Their finding indicates that the folding free energy landscape of this peptide is non-two-state like, allowing for the population of conformational ensembles with different helical lengths and relaxation times in the … Show more

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Cited by 7 publications
(7 citation statements)
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References 83 publications
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“…This hierarchical structural assembly at the molecular level thus necessitates studying how and on what time scales protein secondary structures form in order to understand how proteins achieve their tertiary folds. In this regard, much effort has been devoted to elucidating the folding dynamics and mechanism of α-helix, the most common structural motif found in proteins. The interest in studying the mechanism of α-helix formation is also motivated by the effort to design and develop individually folded, stable α-helices with novel biological functions and/or therapeutic utilities. , …”
Section: Introductionmentioning
confidence: 99%
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“…This hierarchical structural assembly at the molecular level thus necessitates studying how and on what time scales protein secondary structures form in order to understand how proteins achieve their tertiary folds. In this regard, much effort has been devoted to elucidating the folding dynamics and mechanism of α-helix, the most common structural motif found in proteins. The interest in studying the mechanism of α-helix formation is also motivated by the effort to design and develop individually folded, stable α-helices with novel biological functions and/or therapeutic utilities. , …”
Section: Introductionmentioning
confidence: 99%
“…Consequently, the reverse and unfolding process would run in a C-to-N manner. However, experimentally it has been difficult to directly validate this hypothesis due to the fact that there is not a distinct signal that only reports on the nucleation event . Herein, we aim to provide new insights into the α-helix folding mechanism by studying the folding kinetics of three cross-linked, alanine-based peptides using laser-induced temperature-jump ( T -jump) infrared (IR) spectroscopy and molecular dynamics (MD) simulations.…”
Section: Introductionmentioning
confidence: 99%
“…315 ns, whereas the time taken to elongate this nucleus by one residue is position-dependent (ca. 5.9 ns) …”
Section: Vibrational Probesmentioning
confidence: 95%
“…1600 cm −1 . The increased structural resolution via isotopic labeling of selected residues in the peptide sequence allowed Lin et al 86 to show that the T-jump-induced relaxation kinetics of this seemingly simple system not only are complex but also exhibit an unusual initial temperature dependence (when the final temperature is fixed), due to the coexistence of conformational ensembles that have different helicities (Figure 1) as well as the fact that the helical nucleation time constant is ca. 315 ns, whereas the time taken to elongate this nucleus by one residue is position-dependent (ca.…”
Section: Vibrational Probesmentioning
confidence: 99%
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