Measuring Protein Interactions by Optical Biosensors
Copyright policy )Measuring Protein Interactions by Optical Biosensors
AbstractThis unit gives an introduction to the basic techniques of optical biosensing for measuring equilibrium and kinetics of reversible protein interactions. Emphasis is placed on description of robust approaches that will provide reliable results with few assumptions. How to avoid the most commonly encountered problems and artifacts is also discussed. © 2017 by John Wiley & Sons, Inc.
- National Institutes of Health United States
- National Institute of Health Pakistan
- University of Maryland, College Park United States
Immunoassay, Optics and Photonics, Molecular Structure, Surface Properties, Antibody Affinity, Optical Devices, Reproducibility of Results, Proteins, Biosensing Techniques, Models, Theoretical, Models, Biological, Antibodies, Kinetics, Antibody Specificity, Protein Interaction Mapping, Thermodynamics, Immunoprecipitation, Protein Binding
Immunoassay, Optics and Photonics, Molecular Structure, Surface Properties, Antibody Affinity, Optical Devices, Reproducibility of Results, Proteins, Biosensing Techniques, Models, Theoretical, Models, Biological, Antibodies, Kinetics, Antibody Specificity, Protein Interaction Mapping, Thermodynamics, Immunoprecipitation, Protein Binding
selected citations These citations are derived from selected sources.This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).35 popularity This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.Top 10% influence This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).Top 10% impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.Average
Citations provided by BIP!Popularity provided by BIP!