ArticleProceedings of the National Academy of Sciences of the United States of America2010
Hydration dynamics at fluorinated protein surfaces.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
12 citing papers in PubMed, 69 citations in OpenAlex.
- Engineered Proteins and Materials Utilizing Residue-Specific Noncanonical Amino Acid Incorporation.Chemical reviews · 2024Review
- Fluorinated Protein-Ligand Complexes: A Computational Perspective.The journal of physical chemistry. B · 2024Review
- A Robust and Quantitative Reporter System To Evaluate Noncanonical Amino Acid Incorporation in Yeast.ACS synthetic biology · 2018Article
- Enhanced vibrational solvatochromism and spectral diffusion by electron rich substituents on small molecule silanes.The Journal of chemical physics · 2017Article
- A platform for constructing, evaluating, and screening bioconjugates on the yeast surface.Protein engineering, design & selection : PEDS · 2016Article
- Fluorine teams up with water to restore inhibitor activity to mutant BPTI.Chemical science · 2015Article
- Picosecond-resolved fluorescence studies of substrate and cofactor-binding domain mutants in a thermophilic alcohol dehydrogenase uncover an extended network of communication.Journal of the American Chemical Society · 2014Article
- 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
- Article
- An ultrahigh affinity d-peptide antagonist Of MDM2.Journal of medicinal chemistry · 2012Article
- Fluoroalkyl and alkyl chains have similar hydrophobicities in binding to the "hydrophobic wall" of carbonic anhydrase.Journal of the American Chemical Society · 2011Article
- Homoisoleucine: a translationally active leucine surrogate of expanded hydrophobic surface area.Chembiochem : a European journal of chemical biology · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Water-protein interactions dictate many processes crucial to protein function including folding, dynamics, interactions with other biomolecules, and enzymatic catalysis. Here we examine the effect of surface fluorination on water-protein interactions. Modification of designed coiled-coil proteins by incorporation of 5,5,5-trifluoroleucine or (4S)-2-amino-4-methylhexanoic acid enables systematic examination of the effects of side-chain volume and fluorination on solvation dynamics. Using ultrafast fluorescence spectroscopy, we find that fluorinated side chains exert electrostatic drag on neighboring water molecules, slowing water motion at the protein surface.
Indexed as
Identifiers
What OpenQuestion holds
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.