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These hybrid DNA molecules can be then cleaved at the regenerated PstI sites. Its use is not limited to molecular cloning; it is also used in restriction site mapping, genotyping, Southern blotting, restriction fragment length polymorphism (RFLP) and SNP. [9] It is also an isoschizomer restriction enzyme SalPI from Streptomyces albus P. [10]
Structural model at atomic resolution of bacteriophage T4 [1] The structure of a typical myovirus bacteriophage Anatomy and infection cycle of bacteriophage T4.. A bacteriophage (/ b æ k ˈ t ɪər i oʊ f eɪ dʒ /), also known informally as a phage (/ ˈ f eɪ dʒ /), is a virus that infects and replicates within bacteria and archaea.
Cosmids are plasmids that incorporate a segment of bacteriophage λ DNA that has the cohesive end site (cos) which contains elements required for packaging DNA into λ particles. Under apt origin of replication (ori), it can replicate as a plasmid.
Simultaneously the donor strand is ligated to the target strand after cleavage leaving a single strand overhang on either end of the target sequence. These sites usually contain a 5 to 9 base pair overhang that can create a cohesive end. [10] Transposase then holds the sequence in a crossed formation and ligates the donor strand to the target ...
The integration of phage λ takes place at a special attachment site in the bacterial and phage genomes, called att λ. The sequence of the bacterial att site is called attB, between the gal and bio operons, and consists of the parts B-O-B', whereas the complementary sequence in the circular phage genome is called attP and consists of the parts ...
This adapter can be used to convert the cohesive end produced by Bam Hl to one produced by Eco Rl or vice versa. One of its applications is ligating cDNA into a plasmid [ 3 ] or other vectors instead of using Terminal deoxynucleotide Transferase enzyme to add poly A to the cDNA fragment.
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The polymerase is a monomeric protein with two distinct functional domains. Site-directed mutagenesis experiments support the proposition that this protein displays a structural and functional similarity to the Klenow fragment of the Escherichia coli Polymerase I enzyme; [3] it comprises a C-terminal polymerase domain and a spatially separated N-terminal domain with a 3'-5' exonuclease activity.