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Hence, we adopted both radiolabeling and surface plasmon resonance (SPR) techniques to monitor protein adsorption onto the above surfaces.
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This paper presents an optical method for real-time monitoring of protein adsorption using porous silicon self-supported microcavities as a label-free detection platform.
In this report we review the use of ellipsometry in various forms for studies of organic layers with special emphasis on biologically-related issues including in situ monitoring of protein adsorption on planar surfaces and in porous layers, protein monolayer spectroscopy and ellipsometric imaging for determination of thickness distributions.
Accurate monitoring of protein adsorption beyond 24 h is difficult.
Furthermore, complicated microstructures, like porous silicon layers, can be modeled and protein adsorption can be monitored in such layers providing information about pore filling and penetration depths of protein molecules of different size and type.
Using ATR-FT-IR spectroscopic imaging, protein crystallization has been monitored under various solvent conditions simultaneously while protein adsorption and crystallization was studied under a gradient of surface properties.
Subsequent exposure of the PPS PEG/gold pattern to protein adsorption (full human serum) was monitored in situ; SPR-imaging (i-SPR) shows a selective adsorption of proteins on gold, but not on PPS PEG areas.
Next, PEG coatings were created on LP-coated quartz crystals for protein adsorption studies by quartz crystal microbalance with dissipation monitoring (QCM-D).
42 In fact, long-term monitoring of cell attachment has been used as a proxy for long-term protein adsorption.
Despite this, O NDs enable the simultaneous increase in hydrophilicity and protein adsorption affinity.
Results concerning protein adsorption kinetics, viscoelastic properties, crystal lattice parameters and domain formation are presented, and have been obtained with Quartz Crystal Microbalance with Dissipation Monitoring (QCMD) and Atomic Force Microscopy (AFM).
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