ArticleThe journal of physical chemistry letters2020
Unperturbed Detection of the Dynamic Structure in the Hydrophobic Core of Trp-Cage via Two-Dimensional Infrared Spectroscopy.
Article in The journal of physical chemistry letters, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed.
- The Arch from the Stones: Understanding Protein Folding Energy Landscapes via Bioinspired Collective Variables.The journal of physical chemistry letters · 2025Article
- Modulating vibrational energy redistribution in highly conjugated systems.The Journal of chemical physics · 2025Article
- Effect of Main and Side Chains on the Folding Mechanism of the Trp-Cage Miniprotein.ACS omega · 2023Article
- Inhibition of vibrational energy flow within an aromatic scaffold via heavy atom effect.The Journal of chemical physics · 2023Article
- Molecular Vibrational Polariton Dynamics: What Can Polaritons Do?Accounts of chemical research · 2023Article
- Application of a Distance-Dependent Sigmoidal Dielectric Constant to the REMC/SAAP3D Simulations of Chignolin, Trp-Cage, and the G10q Mutant.The protein journal · 2020Article
- Extending the vibrational lifetime of azides with heavy atoms.Physical chemistry chemical physics : PCCP · 2020Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
The tyrosine ring mode is an intrinsic non-perturbing site-specific infrared reporter for conformational dynamics within protein systems. This transition is influenced by direct and indirect interactions associated with the electron-donating ability and the hydrophobicity of the surrounding molecules. Utilizing an intrinsic tyrosine moiety, two-dimensional infrared spectra of Trp-cage, often called the "hydrogen atom" of protein folding, were measured in the folded and denatured states to uncover the dynamics of the hydrophobic core. The vibrational lifetimes and the correlation decays of the tyrosine ring mode showed significant changes upon both temperature and chemical denaturation of the Trp-cage miniprotein, indicating important structural features of the hydrophobic core and its dynamics. The observed Trp6-Tyr3 interactions are in good agreement with the prior studies of the folded state, but they reach beyond the static structure. These stacking interactions and orientations fluctuate on the picosecond time scale as measured through the spectral dephasing within a dehydrated environment.
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Registered trials
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