ArticleBiophysical journal2012
Apparent activation energies associated with protein dynamics on hydrophobic and hydrophilic surfaces.
Article in Biophysical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Temperature-Dependent Dynamic Friction of a Single Human Corneocyte at Nanoscale Contact: An Analytical Approach and Direct Measurement Using Lateral Force Microscopy for Haptic Design Insight.Langmuir : the ACS journal of surfaces and colloids · 2025Article
- Nucleation of protein crystals in pores and their growth.Biophysical reviews · 2025Review
- Single-molecule photocatalytic dynamics at individual defects in two-dimensional layered materials.Science advances · 2021Article
- Adsorption time scales of cluster-forming systems.The European physical journal. E, Soft matter · 2021Article
- A Novel Microscopic Assay Reveals Heterogeneous Regulation of Local Endothelial Barrier Function.Biophysical journal · 2019Article
- Oncological hyperthermia: The correct dosing in clinical applications.International journal of oncology · 2019Article
- Albumin (BSA) adsorption onto graphite stepped surfaces.The Journal of chemical physics · 2017Article
- Protein crystal nucleation in pores.Scientific reports · 2017Article
- Molecular approaches to chromatography using single molecule spectroscopy.Analytical chemistry · 2015Review
- A bottom-up approach to understanding protein layer formation at solid-liquid interfaces.Advances in colloid and interface science · 2014Review
- Interfacial protein-protein associations.Biomacromolecules · 2014Article
- DNA hairpin stabilization on a hydrophobic surface.Small (Weinheim an der Bergstrasse, Germany) · 2013Article
- Identifying mechanisms of interfacial dynamics using single-molecule tracking.Langmuir : the ACS journal of surfaces and colloids · 2012Review
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
With the use of single-molecule total internal reflection fluorescence microscopy (TIRFM), the dynamics of bovine serum albumin (BSA) and human fibrinogen (Fg) at low concentrations were observed at the solid-aqueous interface as a function of temperature on hydrophobic trimethylsilane (TMS) and hydrophilic fused silica (FS) surfaces. Multiple dynamic modes and populations were observed and characterized by their surface residence times and squared-displacement distributions (surface diffusion). Characteristic desorption and diffusion rates for each population/mode were generally found to increase with temperature, and apparent activation energies were determined from Arrhenius analyses. The apparent activation energies of desorption and diffusion were typically higher on FS than on TMS surfaces, suggesting that protein desorption and mobility were hindered on hydrophilic surfaces due to favorable protein-surface and solvent-surface interactions. The diffusion of BSA on TMS appeared to be activationless for several populations, whereas diffusion on FS always exhibited an apparent activation energy. All activation energies were small in absolute terms (generally only a few kBT), suggesting that most adsorbed protein molecules are weakly bound and move and desorb readily under ambient conditions.
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