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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 TeschkeThe Journal of Biological Chemistry|December 4, 2013
ADP-dependent conformational changes distinguish Mycobacterium tuberculosis SecA2 from SecA1Nadia G D'Lima, Carolyn M TeschkeJournal of Bacteriology|May 20, 2008
ATPase activity of Mycobacterium tuberculosis SecA1 and SecA2 proteins and its importance for SecA2 function in macrophagesJie M Hou, Nadia G D'Lima, Nathan W Rigel, et al.Journal of Virology|February 22, 2019
Architect of Virus Assembly: the Portal Protein Nucleates Procapsid Assembly in Bacteriophage P22Tina Motwani, Carolyn M TeschkeVirology|June 9, 2019
Of capsid structure and stability: The partnership between charged residues of E-loop and P-domain of the bacteriophage P22 coat proteinKunica Asija, Carolyn M TeschkeJournal of Virology|May 10, 2019
A Hydrophobic Network: Intersubunit and Intercapsomer Interactions Stabilizing the Bacteriophage P22 CapsidKunica Asija, Carolyn M TeschkeVirology|September 3, 2003
Folding of phage P22 coat protein monomers: kinetic and thermodynamic propertiesEric Anderson, Carolyn M TeschkeCell Stress & Chaperones|April 20, 2007
GroEL/S substrate specificity based on substrate unfolding propensityKristin N Parent, Carolyn M TeschkeVirology|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 TeschkeCurrent Opinion in Virology|March 12, 2019
The amazing HK97 fold: versatile results of modest differencesRobert L Duda, Carolyn M TeschkePageof 7