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Biochemistry|September 20, 2000
SecA folds via a dimeric intermediateS M Doyle, E H Braswell, C M TeschkeBiochemistry|April 1, 1997
The folded conformation of phage P22 coat protein is affected by amino acid substitutions that lead to a cold-sensitive phenotypeD G Fong, S M Doyle, C M TeschkeCell Stress & Chaperones|September 27, 2000
GroEL binds a late folding intermediate of phage P22 coat proteinM D de Beus, S M Doyle, C M TeschkeBiophysical Journal|May 12, 2009
Polyelectrolyte charge corrected molecular weight and effective charge by sedimentationE H BraswellBiochemistry|March 13, 1999
Aggregation and assembly of phage P22 temperature-sensitive coat protein mutants in vitro mimic the in vivo phenotypeC M TeschkeBiochemistry|May 23, 1995
In vitro folding of phage P22 coat protein with amino acid substitutions that confer in vivo temperature sensitivityC M Teschke, J KingCurrent Opinion in Biotechnology|October 1, 1992
Folding and assembly of oligomeric proteins in Escherichia coliC M Teschke, J KingThe Journal of Biological Chemistry|July 31, 1999
Single amino acid substitutions globally suppress the folding defects of temperature-sensitive folding mutants of phage P22 coat proteinL A Aramli, C M TeschkeBiochemistry|November 26, 1996
Interactions between coat and scaffolding proteins of phage P22 are altered in vitro by amino acid substitutions in coat protein that cause a cold-sensitive phenotypeC M Teschke, D G FongPageof 6