ArticleThe journal of physical chemistry. B2012
Validation of response function construction and probing heterogeneous protein hydration by intrinsic tryptophan.
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 10 papers.
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Who cites it
10 citing papers in PubMed, 20 citations in OpenAlex.
- Environment-Driven Coherent Population Transfer Governs the Ultrafast Photophysics of Tryptophan.Journal of the American Chemical Society · 2022Article
- Ultrafast Dynamics of Water-Protein Coupled Motions around the Surface of Eye Crystallin.Journal of the American Chemical Society · 2020Article
- Dynamics and mechanism of ultrafast water-protein interactions.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Picosecond fluorescence dynamics of tryptophan and 5-fluorotryptophan in monellin: slow water-protein relaxation unmasked.The journal of physical chemistry. B · 2015Article
- Direct determination of resonance energy transfer in photolyase: structural alignment for the functional state.The journal of physical chemistry. A · 2014Article
- Article
- Implementing electrostatic polarization cannot fill the gap between experimental and theoretical measurements for the ultrafast fluorescence decay of myoglobin.Journal of molecular modeling · 2014Article
- Quenching Dynamics of Ultraviolet-Light Perception by UVR8 Photoreceptor.The journal of physical chemistry letters · 2014Article
- Origin of tryptophan fluorescence lifetimes. Part 2: fluorescence lifetimes origin of tryptophan in proteins.Journal of fluorescence · 2014Article
- Direct probing of solvent accessibility and mobility at the binding interface of polymerase (Dpo4)-DNA complex.The journal of physical chemistry. A · 2013Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Protein solvation dynamics usually occur on multiple time scales with site specificity, and the characterization of such heterogeneous dynamics requires a convenient optical probe. We proposed a tryptophan methodology, and with site-directed mutagenesis we can use a tryptophan scan to probe any desirable position around protein surfaces. Here, we report our extended solvation model for construction of response functions for probes such as tryptophan with multiple emission peaks and lifetimes. We show our systematic construction procedure and careful analyses of the possible missing percentage of an initial ultrafast component with the established zero-time emission spectrum and limited temporal resolution through two methods of the direct mapping of femtosecond-resolved fluorescence spectra (3D FRES) and the constructed FRES (2D) from the fluorescence transients. We unambiguously validate our extended model with reexamination of solvation dynamics (methanol, water, and proteins) using conventional dye coumarin, intrinsic tryptophan, and cofactor flavin. Using mutant proteins of GB1, we show again the generality of the powerful probe tryptophan for protein hydration (solvation) and the slowdown of the hydration layer dynamics especially at the water-protein interface. These results justify the necessity of our extended solvation model, clarify the confusion of protein hydration in the recent literature, and establish the universal optical probe of tryptophan for heterogeneous protein dynamics.
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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.