Development of a radioimmunoassay for parathion.
exchange mass spectrometry ( DXMS ) subunit type IIß using enhanced amide hydrogen / deuterium Dissecting interdomain communication within cAPK regulatory
To better understand the local and long-range effects that the Arg-to-Lys mutation has on the dynamic properties of the R-subunit, the amide hydrogen/deuterium exchange in the RII subunit was probed by electrospray mass spectrometry.
Some interrelationships of aspartic acid, threonine, and lysine.
Relationship of aspartic acid to pyrimidine biosynthesis.
Cloning, Expression, and Biochemical Characterization of Hexahistidine-tagged Terminase Proteins*
The results suggest that the hexa-His-tagged holoenzyme possesses a mild DNA-binding defect that is masked, at least in part, by integration host factor.
Kinetic characterization of the GTPase activity of phage lambda terminase: evidence for communication between the two "NTPase" catalytic sites of the enzyme.
The data presented here suggest that the two "NTPase" catalytic sites in terminase holoenzyme communicate, and a model describing allosteric interactions between the two sites is proposed.
Kinetic analysis of the endonuclease activity of phage lambda terminase: assembly of a catalytically competent nicking complex is rate-limiting.
Data is presented which demonstrates that phage lambda terminase can efficiently utilize DNA from the closely related phage phi21 as an endonuclease substrate and that the enzyme binds efficiently to the cosB region of both phage genomes.
Cloning, expression, and characterization of a DNA binding domain of gpNu1, a phage lambda DNA packaging protein.
It is proposed that the hydrophobic amino acids found between Lys100 and Pro141 define a self-association domain that is required for the assembly of stable nucleoprotein packaging complexes and that the C-terminal tail of the protein defines a distinct gpA-binding site that is responsible for terminase holoenzyme formation.