Results 61 to 70 of about 347,258 (205)

Identification of critical residues of the serotype modifying O-acetyltransferase of Shigella flexneri [PDF]

open access: yes, 2016
BACKGROUND Thirteen serotypes of Shigella flexneri (S. flexneri) have been recognised, all of which are capable of causing bacillary dysentery or shigellosis. With the emergence of the newer S.
Thanweer, Farzaana, Verma, Naresh K
core   +1 more source

Identification of a key residue for Oligomerisation and pore-formation of Clostridium perfringens NetB [PDF]

open access: yes, 2014
Necrotic enteritis toxin B (NetB) is a β-pore-forming toxin produced by Clostridium perfringens and has been identified as a key virulence factor in the pathogenesis of avian necrotic enteritis, a disease causing significant economic damage to the ...
Basak, Ajit K.   +6 more
core   +2 more sources

Creating Randomized Amino Acid Libraries with the QuikChange® Multi Site-Directed Mutagenesis Kit

open access: yesBioTechniques, 2002
The QuikChange® Multi Site-Directed Mutagenesis Kit is a simple and efficient method for introducing point mutations at up to five sites simultaneously in plasmid DNA templates. Here we used the QuikChange Multi kit with degenerate (one codon) primers to
Holly H. Hogrefe   +3 more
doaj   +1 more source

Probing the Electrostatic and Steric Requirements for Substrate Binding in Human Platelet-Type 12-Lipoxygenase. [PDF]

open access: yes, 2019
Human platelet ALOX12 (hALOX12 or h12-LOX) has been implicated in a variety of human diseases. The present study investigates the active site of hALOX12 to more thoroughly understand how it positions the substrate and achieves nearly perfect regio- and ...
Aleem, Ansari Mukhtar   +7 more
core   +2 more sources

Engineering Dehydrated Amino Acid Residues in the Antimicrobial Peptide Nisin [PDF]

open access: yes, 1992
The small antimicrobial peptide nisin, produced by Lactococcus lactis, contains the uncommon amino acid residues dehydroalanine and dehydrobutyrine and five thio ether bridges.
Boot, Hein J.,   +5 more
core   +1 more source

Extensive site-directed mutagenesis reveals interconnected functional units in the alkaline phosphatase active site

open access: yeseLife, 2015
Enzymes enable life by accelerating reaction rates to biological timescales. Conventional studies have focused on identifying the residues that have a direct involvement in an enzymatic reaction, but these so-called ‘catalytic residues’ are embedded in ...
Fanny Sunden   +4 more
doaj   +1 more source

Site directed mutagenesis and purification of the cDNA for human class I aldehyde dehydrogenase : a thesis presented in partial fulfilment of the requirements for the degree of Master of Science at Massey University [PDF]

open access: yes, 1998
Aldehyde dehydrogenase (ALDH) is a key enzyme of alcohol metabolism, removing acetaldehyde which is formed as a product of the alcohol dehydrogenase reaction.
Wansbrough, Erin M
core  

Catalysts on Demand: Selective Oxidations by Laboratory-Evolved Cytochrome P450 BM3 [PDF]

open access: yes, 2009
Efficient catalysts for selective oxidation of C-H bonds using atmospheric oxygen are highly desirable to decrease the economic and environmental costs associated with conventional oxidation processes.
Arnold, Frances H., Lewis, Jared C.
core   +2 more sources

Multiple-site fragment deletion, insertion and substitution mutagenesis by modified overlap extension PCR

open access: yesBiotechnology & Biotechnological Equipment, 2017
Introducing various mutations at multiple specific sites within a gene requires multiple steps of DNA manipulation, which is the initial, but limiting step of protein structure–function studies.
Fanli Zeng   +4 more
doaj   +1 more source

One-Step, Highly Efficient Site-Directed Mutagenesis by Toxic Protein Selection

open access: yesBioTechniques, 2002
A fast and efficient site-directed mutagenesis method has been developed, using the newly constructed plasmid pTPS19, which expresses the toxic CcdB protein originally encoded by the E. coli F plasmid.
W. Xu   +7 more
doaj   +1 more source

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