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Research Techniques Made Simple: Emerging Methods to Elucidate Protein Interactions through Spatial Proximity
- Source :
- Journal of Investigative Dermatology. 137:e197-e203
- Publication Year :
- 2017
- Publisher :
- Elsevier BV, 2017.
-
Abstract
- Interactions between proteins are essential for fundamental cellular processes, and the diversity of such interactions enables the vast variety of functions essential for life. A persistent goal in biological research is to develop assays that can faithfully capture different types of protein interactions to allow their study. A major step forward in this direction came with a family of methods that delineates spatial proximity of proteins as an indirect measure of protein-protein interaction. A variety of enzyme- and DNA ligation-based methods measure protein co-localization in space, capturing novel interactions that were previously too transient or low affinity to be identified. Here we review some of the methods that have been successfully used to measure spatially proximal protein-protein interactions.
- Subjects :
- Proteomics
0301 basic medicine
Biomedical Research
Measure (physics)
Dermatology
Computational biology
Biology
Bioinformatics
Biochemistry
Biophysical Phenomena
Protein–protein interaction
03 medical and health sciences
Low affinity
Simple (abstract algebra)
Protein Interaction Mapping
Humans
Biotinylation
Molecular Biology
Extramural
Cell Membrane
Proteins
DNA
Cell Biology
Enzymes
030104 developmental biology
Research Design
Subjects
Details
- ISSN :
- 0022202X
- Volume :
- 137
- Database :
- OpenAIRE
- Journal :
- Journal of Investigative Dermatology
- Accession number :
- edsair.doi.dedup.....ed7c55f712bd90c6f8ae470bd368fb3a