ArticleThe journal of physical chemistry. B2012
Thermally induced protein unfolding probed by isotope-edited IR spectroscopy.
Article in The journal of physical chemistry. B, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 18 citations in OpenAlex.
- Hydrophobic Collapse in N-Methylacetamide-Water Mixtures.The journal of physical chemistry. A · 2018Article
- Theoretical Sum Frequency Generation Spectroscopy of Peptides.The journal of physical chemistry. B · 2015Article
- Assessment of amide I spectroscopic maps for a gas-phase peptide using IR-UV double-resonance spectroscopy and density functional theory calculations.The Journal of chemical physics · 2014Article
- Structural motif of polyglutamine amyloid fibrils discerned with mixed-isotope infrared spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Parallel β-sheet vibrational couplings revealed by 2D IR spectroscopy of an isotopically labeled macrocycle: quantitative benchmark for the interpretation of amyloid and protein infrared spectra.Journal of the American Chemical Society · 2012Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Infrared (IR) spectroscopy has been widely utilized for the study of protein folding, unfolding, and misfolding processes. We have previously developed a theoretical method for calculating IR spectra of proteins in the amide I region. In this work, we apply this method, in combination with replica-exchange molecular dynamics simulations, to study the equilibrium thermal unfolding transition of the villin headpiece subdomain (HP36). Temperature-dependent IR spectra and spectral densities are calculated. The spectral densities correctly reflect the unfolding conformational changes in the simulation. With the help of isotope labeling, we are able to capture the feature that helix 2 of HP36 loses its secondary structure before global unfolding occurs, in agreement with experiment.
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