Biotinylation | Wikipedia audio article
Channel: wikipedia tts
Date: 2019-05-03

This is an audio version of the Wikipedia Article:
https://en.wikipedia.org/wiki/Biotinylation


00:00:18 1 Labeling methods
00:01:26 1.1 Enzymatic biotinylation
00:01:36 1.2 Primary amine biotinylation
00:02:47 1.3 Sulfhydryl biotinylation
00:02:57 1.4 Carboxyl biotinylation
00:04:27 1.5 Glycoprotein biotinylation
00:07:03 1.6 Oligonucleotide biotinylation
00:08:32 1.7 Non-specific biotinylation
00:09:27 2 Purpose
00:10:11 2.1 Purification
00:10:40 2.2 Detection
00:11:35 3 Other uses
00:11:44 4 Determining the extent of biotinylation
00:12:42 4.1 HABA assay
00:13:25 4.2 Streptavidin gel-shift
00:14:48 5 Further reading
00:15:15 6 References
00:15:57 Streptavidin gel-shift
00:16:34 Further reading



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SUMMARY
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In biochemistry, biotinylation is the process of covalently attaching biotin to a protein, nucleic acid or other molecule. Biotinylation is rapid, specific and is unlikely to disturb the natural function of the molecule due to the small size of biotin (MW = 244.31 g/mol).  Biotin binds to streptavidin and avidin with an extremely high affinity, fast on-rate, and high specificity, and these interactions are exploited in many areas of biotechnology to isolate biotinylated molecules of interest.  Biotin-binding to streptavidin and avidin is resistant to extremes of heat, pH and proteolysis, making capture of biotinylated molecules possible in a wide variety of environments.  Also, multiple biotin molecules can be conjugated to a protein of interest, which allows binding of multiple streptavidin, avidin or neutravidin protein molecules and increases the sensitivity of detection of the protein of interest.  There is a large number of biotinylation reagents available that exploit the wide range of possible labelling methods. Due to the strong affinity between biotin and streptavidin, the purification of biotinylated proteins has been a widely used approach to identify protein-protein interactions and post-translational events such as ubiquitylation in molecular biology.