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Expression and Purification of Collagen-Like Proteins of Group A Streptococcus
- Source :
- Methods Mol Biol, Methods in Molecular Biology ISBN: 9781071604663
- Publication Year :
- 2020
-
Abstract
- Prokaryotic proteins with extended collagen domain are found in many bacterial species that are pathogenic to humans and animals. The collagen domain is often fused to additional ligand-binding domains and plays both structural and functional roles in modular "bacterial collagens." Here, we describe the step-by-step expression and purification of the recombinant streptococcal collagen-like proteins, rScl, using the Strep-tag II system. The integrity and structural characterization of recombinant collagen-like proteins is very important for defining their function.
- Subjects :
- 0301 basic medicine
Streptococcus pyogenes
02 engineering and technology
medicine.disease_cause
Protein Engineering
Group A
Article
Chromatography, Affinity
law.invention
03 medical and health sciences
Affinity chromatography
Bacterial Proteins
law
medicine
Humans
Amino Acid Sequence
Streptococcus
Chemistry
021001 nanoscience & nanotechnology
Recombinant Proteins
030104 developmental biology
Biochemistry
Recombinant protein production
Recombinant DNA
Collagen
0210 nano-technology
Oligopeptides
Function (biology)
Subjects
Details
- Language :
- English
- ISBN :
- 978-1-07-160466-3
- ISBNs :
- 9781071604663
- Database :
- OpenAIRE
- Journal :
- Methods Mol Biol, Methods in Molecular Biology ISBN: 9781071604663
- Accession number :
- edsair.doi.dedup.....1368f3fbce4175257077fdcba0f18ae4