Surface Plasmon Resonance (SPR)
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The Biacore T200 from Cytiva, detects Surface Plasmon Resonance, an optical technique used to measure binding kinetics and binding equilibrium.
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11 results for "Surface Plasmon Resonance"
11 results for "Surface Plasmon Resonance"
Measuring Molecular Interactions
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A wide array of biomolecular interactions from protein/protein interactions to small molecule ligand/compound binding interactions are important in biology. Fundamentally, there are two ways to measure (or quantify) binding of any of these interactions...
I want to measure a Kd, how do I choose which technique is best?
FAQ
The CMI has four primary technologies to quantify molecular interactions: Surface Plasmon Resonance (SPR) and Biolayer Interferometry (BLI), Isothermal Titration Calorimetry (ITC) and MicroScale Thermophoresis (MST). Each technologies has its advantages...
Hydrophobic Residue in Escherichia coli Thioredoxin Critical for the Processivity of T7 DNA Polymerase
Journal Article
Bacteriophage T7 uses the thioredoxin of its host, Escherichia coli, to enhance the processivity of its DNA polymerase, a requirement for the growth of phage T7. The evolutionarily conserved structure and high degree of homology of amino acid sequence of...
The oncomodulin receptor ArmC10 enables axon regeneration in mice after nerve injury and neurite outgrowth in human iPSC-derived sensory neurons
Journal Article
Oncomodulin (Ocm) is a myeloid cell-derived growth factor that enables axon regeneration in mice and rats after optic nerve injury or peripheral nerve injury, yet the mechanisms underlying its activity are unknown. Using proximity biotinylation...
For a kinetic binding assay using Surface Plasmon Resonance (SPR) or Biolayer Interferometry (BLI), how do I chose which of my binding partners to immobilize?
FAQ
The relative size of the molecules isn't generally the deciding factor. Large proteins will typically give larger signals, but that isn’t necessarily better.
For protein/protein interactions, start by considering other properties of the proteins. Most...
Center for Macromolecular Interactions
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The Center for Macromolecular Interactions The Center for Macromolecular Interactions (CMI) in the department of Biological Chemistry and Molecular Pharmacology at Harvard Medical School has a mission to enhance basic research in the HMS community by...
Grant Support
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Active and potential CMI users and labs may request a letter of support for grant applications, from the CMI Core director, Kelly Arnett . New users should contact the CMI to discuss you project and getting started at the CMI. Existing CMI user labs may...
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Technologies
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To measure a molecular interaction, how do you choose which molecule to be kept at a fixed concentration and which to vary in concentration?
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The choice of which molecule to keep constant and which to vary will depend on the experiment type, the properties of the molecules and the stoichiometry of the interaction.
For ITC, where neither protein is labeled or immobilized, either molecule can be...