Blog
Educational material, comparison studies and publications on SPR and other related techniques for researchers.
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Binding kinetics of glycoprotein interactions using surface plasmon resonance
Surface plasmon resonance (SPR) can be used to analyze all types of interactions ranging from protein-protein, protein-small molecule, protein-nucleic acid, protein-aptamer, protein-lipid, carbohydrate-protein (carbohydrate-lectin) , carbohydrate-carbohydrate and many more. One area of research is the study of glycoprotein binding kinetics, and many scientists are implementing techniques such as SPR to define the kinetic constants of […]
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SPR Expert Interview: Dr. Thorsten Dieckmann
Dr. Thorsten Dieckmann, University of Waterloo Associate Professor in Chemistry and Biochemistry, has used Nicoya’s OpenSPR™ to recently publish “Structural Consequences of Calmodulin EF Hand Mutations” with M. Piazza, V. Taiakina, and J. G. Guillemette. With over 40 publications, we interviewed Dr. Dieckmann about his RNA-ligand research and experience using OpenSPR. He is now expanding […]
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App Note: Binding Kinetics of Protein-Protein Interactions using OpenSPR™
Are protein binding kinetics important for your research? Benchtop SPR is a user-friendly tool that allows researchers to characterize biomolecular interactions in real-time measurements. Forget CO-IPs that days to run and only give end-point measurements, or techniques that use too much precious sample like ITC. In this blog post, we discuss how OpenSPR™ can be […]
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Nicoya’s Q & A: Researcher Profile – Dr. Guy Guillemette
Dr. Guy Guillemette, University of Waterloo Associate Professor in Chemistry and Biochemistry, has used Nicoya’s OpenSPR™ to publish “Structural Studies of a Complex Between Endothelial Nitric Oxide Synthase and Calmodulin at Physiological Calcium Concentration” with M. Piazza and T. Dieckmann. With over 70 publications, we interviewed Dr. Guillemette about his protein-peptide research and experience using […]
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Binding Kinetics of Aptamer Interactions Using Surface Plasmon Resonance
Surface plasmon resonance (SPR) can be used to analyze all types of interactions ranging from protein-protein, protein-small molecule, protein-nucleic acid, protein-aptamer, protein-lipid, carbohydrate-protein and many more. One area of research is the study of aptamer binding kinetics, and many scientists are implementing techniques such as SPR to define the kinetic constants of these types of […]
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A Simple Guide to Choosing the Best Ligand for Your SPR Experiment
Binding and affinity data are key for characterizing molecular interactions, and with benchtop SPR, it has never been easier. Surface Plasmon Resonance (SPR) is a label-free technology which allows researchers to quantitatively analyze binding between two biomolecules. SPR experiments typically consist of a ligand, the biomolecule that is coupled to the sensor surface, and the […]
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What Binding Kinetics Can Tell You That Affinity Can’t
There are many techniques available that can provide scientists with the affinity of an interaction between two biomolecules. The affinity describes how strong the interaction is between two biomolecules. Extremely strong interactions can be on the order of picomolar affinities, while weak interactions can be in the millimolar range, with many interactions falling within this range. Mathematically, the affinity is the concentration of analyte at which half of all binding sites are occupied (at equilibrium conditions).
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Hot New App Note: Temperature Dependent Binding Kinetics of Protein-Protein Interactions Using OpenSPR™
Is temperature dependence important for your binding interactions? In our hot new application note as we demonstrate how OpenSPR’s Temperature Control Add-On can be used to analyze the effect of temperature on the kinetics and affinity of a protein-protein interaction. Surface plasmon resonance (SPR) can be used to analyze all types of interactions including protein-protein, protein-small […]
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Meet the world’s youngest benchtop SPR user: 17-Year-Old Eric Wang
As life science researchers, we all understand the importance of obtaining reliable, consistent binding kinetics for biomolecular interactions. Researchers also know that using SPR to measure these kinetics is the gold-standard technique. However, many researchers face a huge barrier when considering SPR for their projects – SPR has traditionally required a huge learning curve, and […]
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Mastering the Art of Regeneration – The Key to SPR Success
Using surface plasmon resonance to get high-quality binding kinetics is definitely rewarding, but the biggest challenge is often finding the right experimental conditions to get optimal binding kinetics. One of the most important steps to consider is the regeneration step, or more specifically, the regeneration buffer. The regeneration buffer is used to disrupt or reverse the binding between the ligand and analyte, and is often an essential step to getting good kinetics. This can be a tricky task, so we hope that these tips will help you rock your regen! We’ll be going over the principles of regeneration, when to use it, how to optimize it according to your ligand and analyte, and what the resulting benefits are if you execute the steps correctly.