ArticleThe Review of scientific instruments2013
An optics-based variable-temperature assay system for characterizing thermodynamics of biomolecular reactions on solid support.
Article in The Review of scientific instruments, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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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.
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Who cites it
3 citing papers in PubMed.
- Evaluation of Kinetics Using Label-Free Optical Biosensors.Instrumentation science & technology · 2017Article
- Characterization of Receptor Binding Profiles of Influenza A Viruses Using An Ellipsometry-Based Label-Free Glycan Microarray Assay Platform.Biomolecules · 2015Article
- Measuring affinity constants of 1450 monoclonal antibodies to peptide targets with a microarray-based label-free assay platform.Journal of immunological methods · 2015Article
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Authors and funding
9 authors.
Funding
Abstract
A biological state is equilibrium of multiple concurrent biomolecular reactions. The relative importance of these reactions depends on physiological temperature typically between 10 °C and 50 °C. Experimentally the temperature dependence of binding reaction constants reveals thermodynamics and thus details of these biomolecular processes. We developed a variable-temperature opto-fluidic system for real-time measurement of multiple (400-10,000) biomolecular binding reactions on solid supports from 10 °C to 60 °C within ±0.1 °C. We illustrate the performance of this system with investigation of binding reactions of plant lectins (carbohydrate-binding proteins) with 24 synthetic glycans (i.e., carbohydrates). We found that the lectin-glycan reactions in general can be enthalpy-driven, entropy-driven, or both, and water molecules play critical roles in the thermodynamics of these reactions.
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