1993
DOI: 10.1021/bi00091a040 View full text |Buy / Rent full text
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Abstract: Within infected Salmonella cells, newly synthesized 47-kDa phage P22 coat polypeptides fold without covalent modifications into assembly-competent subunits. Coat protein subunits interact with scaffolding protein to form the icosahedral procapsid precursor of the mature, T = 7, virions. In these lattices, the coat subunits form seven classes of local bonding interactions [Prasad, B. V. V., Prevelige, P. E., Marieta, E., Chen, R. O., Thomas, D., King, J., & Chiu, W. (1993) J. Mol. Biol. 231, 65-74]. Coat protei… Show more

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“…To prepare empty procapsid shells that are composed solely of coat protein, the scaffolding protein was removed from the procapsids by repeated extractions with 0.5 M guanidine hydrochloride followed by centrifugation to pellet the shells. The shell stock concentrations were determined by absorbance of the unfolded shell stocks in 6 M guanidine hydrochloride using an extinction coefficient of 0.957 ml mg Ϫ1 cm Ϫ1 at 280 nm (38). All purified empty procapsid shells were suspended in buffer and stored indefinitely at 8.5 mg/ml at 4°C.…”
Section: Methodsmentioning
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rupbmjkragerfmgwileyiopcupepmcmbcthiemesagefrontiersapsiucrarxivemeralduhksmucshluniversity-of-gavle
“…To prepare empty procapsid shells that are composed solely of coat protein, the scaffolding protein was removed from the procapsids by repeated extractions with 0.5 M guanidine hydrochloride followed by centrifugation to pellet the shells. The shell stock concentrations were determined by absorbance of the unfolded shell stocks in 6 M guanidine hydrochloride using an extinction coefficient of 0.957 ml mg Ϫ1 cm Ϫ1 at 280 nm (38). All purified empty procapsid shells were suspended in buffer and stored indefinitely at 8.5 mg/ml at 4°C.…”
Section: Methodsmentioning
“…Purification of coat protein shells was performed as previously described 35 . Coat protein monomers were obtained from urea-denatured empty procapsid shells, as described previously, using dialysis at 4° C against 20 mM sodium phosphate buffer, pH 7.6.…”
Section: Refolded Coat Protein Monomersmentioning
“…35 S-labeled coat protein monomers at 0.5 μM final were mixed with non-labeled coat protein shells at 0.006 and 0.012 μM shells. The samples were incubated at 20 °C and 41 °C for 1 day and separated by sucrose gradient sedimentation.…”
Section: Liquid Scintillation Countingmentioning
“…WT, tsf, and tsf :su coat proteins fold to their native conformation via a 3-state equilibrium folding model, unfolded ⇔ intermediate ⇔ native (U ⇔ I ⇔ N) (Teschke and King 1993;Anderson and Teschke 2003;Doyle et al 2003Doyle et al , 2004. A late-folding intermediate has been identified to interact with GroEL (de Beus et al 2000).…”
Section: Chaperone Roles In Protein Folding and In Capsid Assemblymentioning