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M Teschke

Showing results (11-20 of 86) with videos related to

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Current Opinion in Biotechnology|October 1, 1992
Folding and assembly of oligomeric proteins in Escherichia coliC M Teschke, J King
Plos Pathogens|May 18, 2018
Lessons from bacteriophages part 1: Deriving utility from protein structure, function, and evolutionKunica Asija, Carolyn M Teschke
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
Cell Stress & Chaperones|April 20, 2007
GroEL/S substrate specificity based on substrate unfolding propensityKristin N Parent, Carolyn M Teschke
Journal of Virology|August 14, 2015
A Molecular Staple: D-Loops in the I Domain of Bacteriophage P22 Coat Protein Make Important Intercapsomer Contacts Required for Procapsid AssemblyNadia G D'Lima, Carolyn M Teschke
Virology|July 26, 2011
Bacteriophage P22 capsid size determination: roles for the coat protein telokin-like domain and the scaffolding protein amino-terminusMargaret M Suhanovsky, Carolyn M Teschke
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
Current Opinion in Virology|March 12, 2019
The amazing HK97 fold: versatile results of modest differencesRobert L Duda, Carolyn M Teschke
Pageof 9

Showing results (11-20 of 86) with videos related to

Sort By:
Pageof 9
Current Opinion in Biotechnology|October 1, 1992
Folding and assembly of oligomeric proteins in Escherichia coliC M Teschke, J King
Plos Pathogens|May 18, 2018
Lessons from bacteriophages part 1: Deriving utility from protein structure, function, and evolutionKunica Asija, Carolyn M Teschke
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
Cell Stress & Chaperones|April 20, 2007
GroEL/S substrate specificity based on substrate unfolding propensityKristin N Parent, Carolyn M Teschke
Journal of Virology|August 14, 2015
A Molecular Staple: D-Loops in the I Domain of Bacteriophage P22 Coat Protein Make Important Intercapsomer Contacts Required for Procapsid AssemblyNadia G D'Lima, Carolyn M Teschke
Virology|July 26, 2011
Bacteriophage P22 capsid size determination: roles for the coat protein telokin-like domain and the scaffolding protein amino-terminusMargaret M Suhanovsky, Carolyn M Teschke
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
Current Opinion in Virology|March 12, 2019
The amazing HK97 fold: versatile results of modest differencesRobert L Duda, Carolyn M Teschke
Pageof 9