Fig. 3: Binding and partitioning of AAs in NPM1-RNA and K72-ATP condensates. | Nature Communications

Fig. 3: Binding and partitioning of AAs in NPM1-RNA and K72-ATP condensates.

From: Amino acids bind to phase-separating proteins and modulate biomolecular condensate stability and dynamics

Fig. 3

a The NPM1 protein concentration in the dilute phase after adding glycine at varying concentrations and the fitting curve (solid black) with 95% confidence band (red) using the Langmuir-type binding model; b The fitted binding affinities (Kd) for four different AAs (glycine, proline, serine, and alanine) on K72-ATP condensates (Kd = 0.6 ± 0.2 M for glycine, 1.1 ± 0.4 M for proline, 0.4 ± 0.1 M for serine, and 1.3 ± 0.6 M for alanine); The measured partition coefficients (Kp) by both NMR and LC-MS for three representative AAs (proline, serine, and alanine) in the condensate phase of c. NPM1-RNA systems and d. K72-ATP systems. Data in a and b are from n =  1 independent experiment. Data in b are expressed as mean ± standard deviation of the fitting result, shown in Supplementary Fig. 9. Data in c and d are expressed as mean ± standard deviation of n = 2 independent experiments. Cartoons were created in Biorender (Stellacci, F. (2025) https://BioRender.com/sp9nze0).

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