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C M Teschke

Showing results (1-10 of 15) with videos related to

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Biochemistry|March 13, 1999
Aggregation and assembly of phage P22 temperature-sensitive coat protein mutants in vitro mimic the in vivo phenotypeC M Teschke
Biochemistry|October 12, 1993
Folding of the phage P22 coat protein in vitroC M Teschke, J King
Biochemistry|May 23, 1995
In vitro folding of phage P22 coat protein with amino acid substitutions that confer in vivo temperature sensitivityC M Teschke, J King
Current Opinion in Biotechnology|October 1, 1992
Folding and assembly of oligomeric proteins in Escherichia coliC M Teschke, J King
The 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 Teschke
Biochemistry|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 Fong
The Journal of Biological Chemistry|October 9, 1998
GroEL and GroES control of substrate flux in the in vivo folding pathway of phage P22 coat proteinW S Nakonechny, C M Teschke
Biochemistry|February 2, 2000
Folding defects caused by single amino acid substitutions in a subunit are not alleviated by assemblyC M Capen, C M Teschke
The Journal of Biological Chemistry|April 17, 2001
Alleviation of a defect in protein folding by increasing the rate of subunit assemblyL A Aramli, C M Teschke
Biochemistry|October 12, 1993
Inhibition of viral capsid assembly by 1,1'-bi(4-anilinonaphthalene-5-sulfonic acid)C M Teschke, J King, P E Prevelige
Pageof 2

Showing results (1-10 of 15) with videos related to

Sort By:
Pageof 2
Biochemistry|March 13, 1999
Aggregation and assembly of phage P22 temperature-sensitive coat protein mutants in vitro mimic the in vivo phenotypeC M Teschke
Biochemistry|October 12, 1993
Folding of the phage P22 coat protein in vitroC M Teschke, J King
Biochemistry|May 23, 1995
In vitro folding of phage P22 coat protein with amino acid substitutions that confer in vivo temperature sensitivityC M Teschke, J King
Current Opinion in Biotechnology|October 1, 1992
Folding and assembly of oligomeric proteins in Escherichia coliC M Teschke, J King
The 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 Teschke
Biochemistry|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 Fong
The Journal of Biological Chemistry|October 9, 1998
GroEL and GroES control of substrate flux in the in vivo folding pathway of phage P22 coat proteinW S Nakonechny, C M Teschke
Biochemistry|February 2, 2000
Folding defects caused by single amino acid substitutions in a subunit are not alleviated by assemblyC M Capen, C M Teschke
The Journal of Biological Chemistry|April 17, 2001
Alleviation of a defect in protein folding by increasing the rate of subunit assemblyL A Aramli, C M Teschke
Biochemistry|October 12, 1993
Inhibition of viral capsid assembly by 1,1'-bi(4-anilinonaphthalene-5-sulfonic acid)C M Teschke, J King, P E Prevelige
Pageof 2