Gang Zhao, Ph.D.

Affiliations: 
2005 Stony Brook University, Stony Brook, NY, United States 
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"Gang Zhao"
Mean distance: 4423.67
 

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Erwin London grad student 2005 SUNY Stony Brook
 (Conformational and functional study of diphtheria toxin T domain.)
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Publications

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Wang J, Zhao G, Li M. (2016) Establishment of processing map and analysis of microstructure on multi-crystalline tungsten plastic deformation process at elevated temperature Materials and Design. 103: 268-277
Zhao G, London E. (2009) Strong correlation between statistical transmembrane tendency and experimental hydrophobicity scales for identification of transmembrane helices. The Journal of Membrane Biology. 229: 165-8
Lai B, Zhao G, London E. (2008) Behavior of the deeply inserted helices in diphtheria toxin T domain: helices 5, 8, and 9 interact strongly and promote pore formation, while helices 6/7 limit pore formation. Biochemistry. 47: 4565-74
Zhao G, London E. (2008) Behavior of diphtheria toxin T domain containing substitutions that block normal membrane insertion at Pro345 and Leu307: Control of deep membrane insertion and coupling between deep insertion of hydrophobic subdomains (Biochemistry (2005) 44, 11, (4488-4498)) Biochemistry. 47: 5258
Wu Z, Jakes KS, Samelson-Jones BS, et al. (2006) Protein translocation by bacterial toxin channels: a comparison of diphtheria toxin and colicin Ia. Biophysical Journal. 91: 3249-56
Zhao G, London E. (2006) An amino acid "transmembrane tendency" scale that approaches the theoretical limit to accuracy for prediction of transmembrane helices: relationship to biological hydrophobicity. Protein Science : a Publication of the Protein Society. 15: 1987-2001
Zhao G, London E. (2005) Behavior of diphtheria toxin T domain containing substitutions that block normal membrane insertion at Pro345 and Leu307: control of deep membrane insertion and coupling between deep insertion of hydrophobic subdomains. Biochemistry. 44: 4488-98
Rosconi MP, Zhao G, London E. (2004) Analyzing topography of membrane-inserted diphtheria toxin T domain using BODIPY-streptavidin: at low pH, helices 8 and 9 form a transmembrane hairpin but helices 5-7 form stable nonclassical inserted segments on the cis side of the bilayer. Biochemistry. 43: 9127-39
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