Blog
Educational material, comparison studies and publications on SPR and other related techniques for researchers.
-
Comparison Study of SPR Instruments Using Commercially Relevant Binding Systems
Comparison Study of SPR Instruments Using Commercially Relevant Binding Systems: A protein-protein interaction was analyzed on the OpenSPR™ and the standard SPR insturment. Kinetic analysis was used to determine the on rate, off rate, and affinity constant of the protein-protein interaction. Both data sets generated from OpenSPR™ and the comparison SPR instrument show excellent fits […]
-
Binding Kinetics of Protein-Lipid 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-aptamers, protein-lipids, and many more. One area of research is the study of lipid binding kinetics, and many scientists are implementing techniques such as SPR to define the affinity and specificity of these interactions. Why […]
-
8 Advantages of Using SPR in Your Own Lab
What do you do if you need a specific piece of equipment, but can’t afford to purchase it outright? You may apply for a research grant, ask fellow researchers to borrow their equipment, or avoid conducting the experiments altogether.
-
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 […]
-
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 […]
-
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 […]
-
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 […]
-
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 […]
-
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 […]
-
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).