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We explore how the spectral phase of attosecond pulse trains influences the optical cross section in transient absorption (TA) spectroscopy. The interaction of extreme ultraviolet (XUV) and time-delayed near-infrared (NIR) fields with an atomic or molecular system governs the dynamics. As already shown in RABBITT experiments (Reconstruction of Attosecond Beating by Interference of Two-Photon Transitions), the spectral phase of the XUV pulses can be extracted from the photoionization spectrum as a function of the time delay. Similarly, this XUV phase imprints itself on delay-dependent optical cross-section oscillations. With a perturbative analytical approach and by simulating the quantum dynamics both in a few-level model and via solving the time-dependent Schrödinger equation for atomic hydrogen, we reveal the similarity between the spectral phase in RABBITT and TA spectroscopy. Published by the American Physical Society2025
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Predicting the Morphology of Multiphase Biomolecular Condensates from Protein Interaction Networks
Phase-separated biomolecular condensates containing proteins and RNAs can assemble into higher-order structures by forming thermodynamically stable interfaces between immiscible phases. Using a minimal model of a protein/RNA interaction network, we demonstrate how a “shared” protein species that partitions into both phases of a multiphase condensate can function as a tunable surfactant that modulates the interfacial properties. We use Monte Carlo simulations and free-energy calculations to identify conditions under which a low concentration of this shared species is sufficient to trigger a wetting transition. We also describe a numerical approach based on classical density functional theory to predict concentration profiles and surface tensions directly from the model protein/RNA interaction network. Finally, we show that the wetting phase diagrams that emerge from our calculations can be understood in terms of a simple model of selective adsorption to a fluctuating interface. Our work shows how a low-concentration protein species might function as a biological switch for regulating multiphase condensate morphologies. Published by the American Physical Society2024
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- Award ID(s):
- 2143670
- PAR ID:
- 10565938
- Publisher / Repository:
- American Physical Society
- Date Published:
- Journal Name:
- PRX Life
- Volume:
- 2
- Issue:
- 2
- ISSN:
- 2835-8279
- Format(s):
- Medium: X
- Sponsoring Org:
- National Science Foundation
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- Free Publicly Accessible Full Text
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Accepted Manuscript1.0
- Journal Article:
- https://doi.org/10.1103/PRXLife.2.023013
