ArticleInternational journal of molecular sciences2026
Dielectric Response of Micelles Built from Intrinsically Disordered Beta-Casein.
Article in International journal of molecular sciences, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
For many decades, protein function was associated with a rigid three-dimensional structure. However, in recent years, interest has grown rapidly in proteins that successfully perform their functions despite being intrinsically disordered. Unfortunately, to date, insufficient structural information has been collected on this novel protein family to analyze its structure-function correlations. To obtain the required structural information on intrinsically disordered beta-casein (b-CN), we used broadband dielectric spectroscopy, which has long been used to study structured proteins. Dielectric measurements in the frequency range from 1 Hz to 67 GHz detected three Cole-Cole relaxation processes in a micellar solution of disordered beta-casein. The experimental data obtained were used to estimate the dynamical hierarchy of dipole-dipole correlations involved in the relaxation of each dipole component of the system. The dielectric relaxation of micellized disordered b-CN is rather complex, indicating the cascade nature of protein relaxation, which involves long-range structural correlations of flexible charged protein chains. The relaxation of free and bound water is close to the Debye type, which is entirely consistent with the "wait and switch" model of dielectric relaxation, in which a water dipole waits for the arrival of a structural or ionic defect for reorientation. The relaxation rates of the two water fractions differ dramatically, with bound-water relaxation being two orders of magnitude slower than free-water relaxation. The most reasonable explanation for this difference probably lies in the spatial confinement of bound water resulting from the influence of the charged protein surface. The results obtained demonstrate the research potential of broadband dielectric spectroscopy not only for long-studied rigid, structured proteins with permanent dipole moments but also for the novel family of disordered proteins with fluctuating dipole moments.
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.