ArticleThe journal of physical chemistry. B2007
Measurement of solvation responses at multiple sites in a globular protein.
Article in The journal of physical chemistry. B, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 111 citations in OpenAlex.
- Precision Labeling of Native Antibodies with Lock Coupling.Journal of the American Chemical Society · 2026Article
- A Foundational Shift in Models for Enzyme Function.Journal of the American Chemical Society · 2025Review
- Temporal Resolution of Activity-Related Solvation Dynamics in the TIM Barrel Enzyme Murine Adenosine Deaminase.ACS catalysis · 2024Article
- Temporal and spatial resolution of distal protein motions that activate hydrogen tunneling in soybean lipoxygenase.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Dynamical activation of function in metalloenzymes.FEBS letters · 2023Review
- Influence of crowding agents on the dynamics of a multidomain protein in its denatured state: a solvation approach.European biophysics journal : EBJ · 2020Article
- Detecting and Characterizing the Kinetic Activation of Thermal Networks in Proteins: Thermal Transfer from a Distal, Solvent-Exposed Loop to the Active Site in Soybean Lipoxygenase.The journal of physical chemistry. B · 2019Article
- Picosecond fluorescence dynamics of tryptophan and 5-fluorotryptophan in monellin: slow water-protein relaxation unmasked.The journal of physical chemistry. B · 2015Article
- Dynamically achieved active site precision in enzyme catalysis.Accounts of chemical research · 2015Review
- Picosecond-resolved fluorescent probes at functionally distinct tryptophans within a thermophilic alcohol dehydrogenase: relationship of temperature-dependent changes in fluorescence to catalysis.The journal of physical chemistry. B · 2014Article
- Implementing electrostatic polarization cannot fill the gap between experimental and theoretical measurements for the ultrafast fluorescence decay of myoglobin.Journal of molecular modeling · 2014Article
- Calculations of the electric fields in liquid solutions.The journal of physical chemistry. B · 2013Article
- Validation of response function construction and probing heterogeneous protein hydration by intrinsic tryptophan.The journal of physical chemistry. B · 2012Article
- Femtosecond conical intersection dynamics of tryptophan in proteins and validation of slowdown of hydration layer dynamics.Journal of the American Chemical Society · 2012Article
- Quantitative, directional measurement of electric field heterogeneity in the active site of ketosteroid isomerase.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Molecular description of flexibility in an antibody combining site.The journal of physical chemistry. B · 2010Article
- Solvation response along the reaction coordinate in the active site of ketosteroid isomerase.Journal of the American Chemical Society · 2010Article
- Profiling of dynamics in protein-lipid-water systems: a time-resolved fluorescence study of a model membrane protein with the label BADAN at specific membrane depths.European biophysics journal : EBJ · 2010Article
- Site-directed fluorescence labeling of a membrane protein with BADAN: probing protein topology and local environment.Biophysical journal · 2008Article
- Ultrafast fluorescence spectroscopy via upconversion applications to biophysics.Methods in enzymology · 2008Review
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Proteins respond to electrostatic perturbations through complex reorganizations of their charged and polar groups, as well as those of the surrounding media. These solvation responses occur both in the protein interior and on its surface, though the exact mechanisms of solvation are not well understood, in part because of limited data on the solvation responses for any given protein. Here, we characterize the solvation kinetics at sites throughout the sequence of a small globular protein, the B1 domain of streptococcal protein G (GB1), using the synthetic fluorescent amino acid Aladan. Aladan was incorporated into seven different GB1 sites, and the time-dependent Stokes shift was measured over the femtosecond to nanosecond time scales by fluorescence upconversion and time-correlated single photon counting. The seven sites range from buried within the protein core to fully solvent-exposed on the protein surface, and are located on different protein secondary structures including beta-sheets, helices, and loops. The dynamics in the protein sites were compared against the free fluorophore in buffer. All protein sites exhibited an initial, ultrafast Stokes shift on the subpicosecond time scale similar to that observed for the free fluorophore, but smaller in magnitude. As the probe is moved from the surface to more buried sites, the dynamics of the solvation response become slower, while no clear correlation between dynamics and secondary structure is observed. We suggest that restricted movements of the surrounding protein residues give rise to the observed long time dynamics and that such movements comprise a large portion of the protein's solvation response. The proper treatment of dynamic Stokes shift data when the time scale for solvation is comparable to the fluorescence lifetime is discussed.
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