A Mathematical Model for the Description of the Coomassie Brilliant Blue Protein Assay

Atherton, B.A.; Cunningham, Eithne; Splittgerber, A.

doi:10.1006/abio.1996.0024

Cited by 23 publications

(17 citation statements)

References 5 publications

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“…Equations [4] and [5] predict that the extent of protein precipitation will exhibit a bell-shaped dependence on the total protein concentration when the total tannin is held constant. As an example, Fig.…”

Section: Resultsmentioning

confidence: 99%

“…Numerical analysis of Eqs. [3]- [5] also shows that when n ϫ P t ӷ r ϫ T t , K Ϫ 1 , the average number of tannic acid molecules per each protein molecule at the point of maximum precipitation is related to l by the relation r ϫ T t /P t Ϸ 1.25 ϫ l. This simple relation gives a lower limit of the value of l; when r ϭ 5 (see below), one obtains from the data in Fig. 1, l Ն 11.…”

Section: Resultsmentioning

confidence: 99%

“…Macromolecule-ligand binding is studied by variety of techniques, such as equilibrium dialysis (8), absorption spectroscopy (5,6,9) and calorimetry (10). Ordinarily, the number of moles of ligands bound per mole of protein is obtained as a function of unbound ligand concentration, and the data are treated by using a mathematical model in which the protein is assumed to have a fixed number of equivalent binding sites.…”

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confidence: 99%

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A Mathematical Model Describing Tannin–Protein Association

Silber

Davitt

Khairutdinov

et al. 1998

Analytical Biochemistry

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

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confidence: 99%

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A Mathematical Model Describing Tannin–Protein Association

Silber

Davitt

Khairutdinov

et al. 1998

Analytical Biochemistry

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“…To obtain accurate estimates, all densitometry results for the four proteins were plotted and the amounts calculated from the initial, linear parts of the curves. These values were further corrected for the disparities in arginine-plus-lysine content between the proteins, as indicated previously (1). Errors were estimated from the deviations in the linear fits.…”

Section: Methodsmentioning

confidence: 99%

Packaging Accessory Protein P7 and Polymerase P2 Have Mutually Occluding Binding Sites inside the Bacteriophage ϕ6 Procapsid

Němeček

Qiao²,

Mindich³

et al. 2012

J Virol

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Bacteriophage 6 is a double-stranded RNA (dsRNA) virus whose genome is packaged sequentially as three single-stranded RNA (ssRNA) segments into an icosahedral procapsid which serves as a compartment for genome replication and transcription. The procapsid shell consists of 60 copies each of P1 A and P1 B , two nonequivalent conformers of the P1 protein. Hexamers of the packaging ATPase P4 are mounted over the 5-fold vertices, and monomers of the RNA-dependent RNA polymerase (P2) attach to the inner surface, near the 3-fold axes. A fourth protein, P7, is needed for packaging and also promotes assembly. We used cryo-electron microscopy to localize P7 by difference mapping of procapsids with different protein compositions. We found that P7 resides on the interior surface of the P1 shell and appears to be monomeric. Its binding sites are arranged around the 3-fold axes, straddling the interface between two P1 A subunits. Thus, P7 may promote assembly by stabilizing an initiation complex. Only about 20% of the 60 P7 binding sites were occupied in our preparations. P7 density overlaps P2 density similarly mapped, implying mutual occlusion. The known structure of the 12 homolog fits snugly into the P7 density. Both termini-which have been implicated in RNA binding-are oriented toward the adjacent 5-fold vertex, the entry pathway of ssRNA segments. Thus, P7 may promote packaging either by interacting directly with incoming RNA or by modulating the structure of the translocation pore.

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“…15,16) Measurement of White Blood Cell Count (WBC) A blood aliquot was collected, and WBC was determined with a Coulter counter (Coulter STKS, Hialeah, FL, U.S.A.).…”

Section: Measurement Of Total Protein In Pleural Fluidmentioning

confidence: 99%