Eric D. Foley
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View article: Mass photometry enables label-free tracking and mass measurement of single proteins on lipid bilayers
Mass photometry enables label-free tracking and mass measurement of single proteins on lipid bilayers Open
The quantification of membrane-associated biomolecular interactions is crucial to our understanding of various cellular processes. State-of-the-art single-molecule approaches rely largely on the addition of fluorescent labels, which compli…
View article: Frontispiz: Quantifying Protein–Protein Interactions by Molecular Counting with Mass Photometry
Frontispiz: Quantifying Protein–Protein Interactions by Molecular Counting with Mass Photometry Open
Protein-Protein-Wechselwirkungen In der Zuschrift auf S. 10866 führen P. Kukura, W. B. Struwe et al. molekulares Zählen mittels Massenphotometrie als eine Methode zur Quantifizierung von Protein-Protein-Wechselwirkungen ein. Bindungsaffini…
View article: Frontispiece: Quantifying Protein–Protein Interactions by Molecular Counting with Mass Photometry
Frontispiece: Quantifying Protein–Protein Interactions by Molecular Counting with Mass Photometry Open
Protein–Protein Interactions In their Communication on page 10774, P. Kukura, W. B. Struwe et al. introduce molecular counting with mass photometry as a method for quantifying protein–protein interactions. Binding affinities and associated…
View article: Quantifying Protein–Protein Interactions by Molecular Counting with Mass Photometry
Quantifying Protein–Protein Interactions by Molecular Counting with Mass Photometry Open
Interactions between biomolecules control the processes of life in health and their malfunction in disease, making their characterization and quantification essential. Immobilization‐ and label‐free analytical techniques are desirable beca…
View article: Quantifying Protein–Protein Interactions by Molecular Counting with Mass Photometry
Quantifying Protein–Protein Interactions by Molecular Counting with Mass Photometry Open
Interactions between biomolecules control the processes of life in health and their malfunction in disease, making their characterization and quantification essential. Immobilization‐ and label‐free analytical techniques are desirable beca…
View article: Quantifying protein-protein interactions by molecular counting with mass photometry
Quantifying protein-protein interactions by molecular counting with mass photometry Open
Interactions between biomolecules control the processes of life in health, and their malfunction in disease, making their characterization and quantification essential. Immobilization- and label-free analytical techniques are particular de…
View article: CCDC 1839151: Experimental Crystal Structure Determination
CCDC 1839151: Experimental Crystal Structure Determination Open
An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available …
View article: Structure–function relationships of donor–acceptor Stenhouse adduct photochromic switches
Structure–function relationships of donor–acceptor Stenhouse adduct photochromic switches Open
Surprisingly small structural changes in Donor–Acceptor Stenhouse Adducts (DASAs) result in predictable, robust and effective photochromic switches.
View article: CCDC 1839150: Experimental Crystal Structure Determination
CCDC 1839150: Experimental Crystal Structure Determination Open
An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available …
View article: CCDC 1839152: Experimental Crystal Structure Determination
CCDC 1839152: Experimental Crystal Structure Determination Open
An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available …
View article: CCDC 1839149: Experimental Crystal Structure Determination
CCDC 1839149: Experimental Crystal Structure Determination Open
An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available …
View article: CCDC 1839144: Experimental Crystal Structure Determination
CCDC 1839144: Experimental Crystal Structure Determination Open
An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available …
View article: CCDC 1839148: Experimental Crystal Structure Determination
CCDC 1839148: Experimental Crystal Structure Determination Open
An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available …
View article: CCDC 1839145: Experimental Crystal Structure Determination
CCDC 1839145: Experimental Crystal Structure Determination Open
An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available …
View article: CCDC 1839146: Experimental Crystal Structure Determination
CCDC 1839146: Experimental Crystal Structure Determination Open
An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available …
View article: CCDC 1839147: Experimental Crystal Structure Determination
CCDC 1839147: Experimental Crystal Structure Determination Open
An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available …