ArticleThe journal of physical chemistry. B2012
Fast dynamics of HP35 for folded and urea-unfolded conditions.
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 9 papers.
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Who cites it
9 citing papers in PubMed.
- Unfolding of the Villin Headpiece Domain: Revealing Structural Heterogeneity with Time-Resolved X-Ray Solution Scattering and Markov State Modeling.Chemphyschem : a European journal of chemical physics and physical chemistry · 2025Article
- Transparent window 2D IR spectroscopy of proteins.The Journal of chemical physics · 2021Review
- Protein Dynamics by Two-Dimensional Infrared Spectroscopy.Annual review of analytical chemistry (Palo Alto, Calif.) · 2021Article
- Deuteration of nonexchangeable protons on proteins affects their thermal stability, side-chain dynamics, and hydrophobicity.Protein science : a publication of the Protein Society · 2020Article
- Site-Specific 1D and 2D IR Spectroscopy to Characterize the Conformations and Dynamics of Protein Molecular Recognition.The journal of physical chemistry. B · 2019Article
- Watching Proteins Wiggle: Mapping Structures with Two-Dimensional Infrared Spectroscopy.Chemical reviews · 2017Review
- Infrared and fluorescence assessment of the hydration status of the tryptophan gate in the influenza A M2 proton channel.Physical chemistry chemical physics : PCCP · 2016Article
- C≡N stretching vibration of 5-cyanotryptophan as an infrared probe of protein local environment: what determines its frequency?Physical chemistry chemical physics : PCCP · 2016Article
- Microscopic insights into the protein-stabilizing effect of trimethylamine N-oxide (TMAO).Proceedings of the National Academy of Sciences of the United States of America · 2014Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
The changes in fast dynamics of HP35 with a double CN vibrational dynamics label (HP35-P(2)) as a function of the extent of denaturation by urea were investigated with two-dimensional infrared (2D IR) vibrational echo spectroscopy. Cyanophenylalanine (PheCN) replaces the native phenylalanine at two residues in the hydrophobic core of HP35, providing vibrational probes. NMR data show that HP35-P(2) maintains the native folded structure similar to wild type and that both PheCN residues share essentially the same environment within the peptide. A series of time-dependent 2D IR vibrational echo spectra were obtained for the folded peptide and the increasingly unfolded peptide. Analysis of the time dependence of the 2D spectra yields the system's spectral diffusion, which is caused by the sampling of accessible structures of the peptide under thermal equilibrium conditions. The structural dynamics become faster as the degree of unfolding is increased.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.