What is chitin binding domain?
What is chitin binding domain?
Definition. Protein which binds chitin, a linear polysaccharide consisting of (1->4)-beta-linked D-glucosamine residues, most of which are N-acetylated. The 30-43 amino acids long chitin-binding domain contains several conserved glycine and cysteines residues. The conserved cysteines form disulfide bonds.
How does Intein cleavage work?
An intein (intervening protein) carries out a unique auto-processing event known as protein splicing in which it excises itself out from a larger precursor polypeptide through the cleavage of two peptide bonds and, in the process, ligates the flanking extein (external protein) sequences through the formation of a new …
Where does protein splicing occur?
But, unlike RNA splicing which occurs at the level of an RNA precur- sor, protein splicing is a self-catalyzed process occurring on the level of the polypeptide in which an intervening polypeptide domain called an intein (int[ernal] [protlein) [l] is precisely excised from a precursor polypeptide.
Why does protein splicing occur?
Protein splicing is an intramolecular reaction of a particular protein in which an internal protein segment (called an intein) is removed from a precursor protein with a ligation of C-terminal and N-terminal external proteins (called exteins) on both sides. Normally, splicing is associated only with pre-mRNA splicing.
How does chitinases work as a defense mechanism?
Chitinases can enhance the plant’s defense system as they act on chitin, a major component of the cell wall of pathogenic fungi, and render the fungi inactive without any negative impact on the plants. Along with strengthening plant defense mechanisms, chitinases also improve plant growth and yield.
How does chitin differ from cellulose in structure and function?
The key difference between cellulose and chitin is that cellulose is the significant structural polymer in the primary cell walls of the plant cells while chitin is the main structural polymer found in the fungal cell wall.
What is the principle of affinity chromatography?
The principle of affinity chromatography is that the stationary phase consists of a support medium (e.g. cellulose beads) on which the substrate (or sometimes a coenzyme) has been bound covalently, in such a way that the reactive groups that are essential for enzyme binding are exposed.
What occurs during the process of bacterial protein splicing?
Protein splicing is a posttranslational processing event that involves the precise removal of an internal polypeptide segment, termed an intein, from a precursor protein with the concomitant ligation of the flanking polypeptide sequences, termed exteins.
What is Neb’s approach to ethics?
New England Biolabs (NEB) is committed to practicing ethical science – we believe it is our job as researchers to ask the important questions that when answered will help preserve our quality of life and the world that we live in. However, this research should always be done in safe and ethical manner. Learn more .
What is the function of CBD in intein tag?
Each intein tag contains a chitin binding domain (CBD) for the affinity purification of the fusion protein on chitin resin (2–4). Induction of on-column cleavage, using thiol reagents such as dithiothreitol (DTT), releases the target protein from the intein tag (Figures 1,2).
What is the binding capacity of the CBD-fusion protein?
Binding capacity: 2 mg maltose-binding protein/mL bed volume released from the resin after cleavage of the maltose-binding-CBD-fusion protein For larger volume requirements, customized and bulk packaging is available by purchasing through the OEM/Bulks department at NEB.
