Closure to “Investigation of Sewer-Line Failure” by Steven C. Helfrich

Helfrich, Steven C.

doi:10.1061/(asce)0887-3828(1998)12:3(168)

Cited by 1 publication

(2 citation statements)

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“…Light Scattering. Determinations of molecular weight and hydrodynamic radii characterizations were performed on a Waters 600 HPLC system equipped with a PDI2020/DLS light scattering detector (Precision Detectors Inc.) embedded in the thermostated chamber of a Waters 2440 differential refractometer (30). Protein concentrations in the eluted peaks were determined by a standard HPLC UV detector using the absorbance at 280 nm and the extinction coefficients reported below.…”

Section: Methodsmentioning

confidence: 99%

“…The 90°light scattering detector was calibrated using BSA (mass 66 400 Da, dn/dc ) 0.187 mL/ g, 280 ) 0.647 cm 2 /mg) as a standard. Mass distributions as well as hydrodynamic radii were computed using the software provided by the manufacturer [PrecisionAnalyze, (30)]. All experiments were performed at 30 °C unless indicated otherwise, and the hydrodynamic parameters were corrected for buffer viscosity and temperature.…”

Section: Methodsmentioning

confidence: 99%

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Assembly of Bacteriophage PRD1 Spike Complex: Role of the Multidomain Protein P5

2000

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The spike structure of bacteriophage PRD1 is comprised of proteins P2, P5, and P31. It resembles the corresponding receptor-binding structure of adenoviruses. We show that purified recombinant protein P5 is an elongated (30 x 2.7 nm; R(h) = 5.5 nm), multidomain trimer which can slowly associate into nonamers. Cleavage of the 340 amino acid long P5 with collagenase yields 2 fragments. The larger, 205 amino acid long C-terminal fragment appears to contain the residues responsible for the trimerization of the protein, whereas the smaller N-terminal part mediates the interaction of P5 with the pentameric vertex protein P31 (24 x 2.5 nm, R(h) = 4.2 nm). In addition, the presence of the N-terminal sequence is required for the formation of the P5 nonamer. The results presented here suggest that P5 and P31 form an elongated adaptor complex at the 5-fold vertexes of the virion which anchors the adsorption protein P2 (21 x 2.5 nm; R(h) = 4.1 nm). Our results also suggest that the P5 trimer forms a substantial part of the viral spike shaft that was previously thought to be composed exclusively of protein P2.

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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%