computer program dynafit (BioKin Ltd)
90
Structured Review
BioKin Ltd
computer program dynafit
Computer Program Dynafit, supplied by BioKin Ltd, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/program+dynafit/computer+program+dynafit/pm19378562-145-19-22
Average 90 stars, based on 1 article reviews
Computer Program Dynafit, supplied by BioKin Ltd, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/program+dynafit/computer+program+dynafit/pm19378562-145-19-22
Average 90 stars, based on 1 article reviews
computer program dynafit - by Bioz Stars,
2026-09
90/100 stars
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other:Article Title: Program DYNAFIT for the analysis of enzyme kinetic data: application to HIV proteinase. Article Snippet: factory fit of more than one progress curve to the same A computer program with the code name DYNAFIT set of rate constants, and it can be used for active-site was developed for fitting either the initial velocities titrations.. Finally, DYNAFIT can treat as adjustable paor the time course of enzyme reactions to an arbitrary rameters certain instrumental parameters, such as basemolecular mechanism represented symbolically by a line signal or molar absorptivity. set of chemical equations.. Seven numerical tests and Classical enzyme kinetics (3–5) is concerned with five graphical tests are applied to judge the goodness fitting a set experimental data to a single algebraic of fit. Article Title: Transition from octahedral to tetrahedral geometry causes the activation or inhibition by Znf2+ of Pseudomonas aeruginosa phosphorylcholine phosphatase. Article Snippet: Pseudomonas aeruginosa phosphorylcholine phosphatase (PchP) catalyzes the hydrolysis of phosphorylcholine, which is produced by the action of hemolytic phospholipase C on phosphatidylcholine or sphyngomielin, to generate choline and inorganic phosphate.. Among divalent cations, its activity is dependent on Mg or Zn.. Mg produced identical activation at pH 5.0 and 7.4, but Zn was an activator at pH 5.0 and became an inhibitor at pH 7.4. Construct:Article Title: The N-terminal soluble domains of Bacillus subtilis CopA exhibit a high affinity and capacity for Cu(I) ions. Article Snippet: CopA from Bacillus subtilis is a Cu(I)-transporting P-type ATPase involved in resistance to high levels of environmental copper.. At its N-terminus are two soluble domains, a and b, that, when generated in isolation from the membrane part, have previously been shown to exhibit unusual Cu(I)-binding behaviour: at >1 Cu(I) per CopAab the protein dimerises, resulting in the formation of a species with luminescence properties characteristic of a solvent-shielded Cu(I) cluster.. Further insight into the Cu(I)-binding properties of CopAab are now reported. |