Hongli Zhan, Ph.D.

Affiliations: 
Rice University, Houston, TX 
Area:
Structure and function of genetic regulatory proteins
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"Hongli Zhan"
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Parents

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Kathleen S. Matthews grad student 2005 Rice University
 (Biophysical characterization of the allosteric transition in lactose repressor protein (LacI).)
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Publications

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Xu JS, Hewitt MN, Gulati JS, et al. (2018) Lactose Repressor Hinge Domain Independently Binds DNA. Protein Science : a Publication of the Protein Society
Swint-Kruse L, Tungtur S, Zhan H, et al. (2013) In Vitro Thermodynamics of DNA Binding Correlate with In Vivo Transcription Repression by a Synthetic Laci/Galr Paralog Biophysical Journal. 104: 576a
Tungtur S, Skinner H, Zhan H, et al. (2011) In vivo tests of thermodynamic models of transcription repressor function. Biophysical Chemistry. 159: 142-51
Swint-Kruse L, Manley M, Tungtur S, et al. (2011) Correlating in Vitro Measurements of Protein-DNA Binding Affinities with in Vivo Repression and Impact on the Growth Rate of the Host Organism Biophysical Journal. 100: 321a
Zhan H, Camargo M, Matthews KS. (2010) Positions 94-98 of the lactose repressor N-subdomain monomer-monomer interface are critical for allosteric communication. Biochemistry. 49: 8636-45
Rutkauskas D, Zhan H, Matthews KS, et al. (2010) Dna Looping By Lactose Repressor Requires Tetramer Opening Biophysical Journal. 98: 72a
Rutkauskas D, Zhan H, Matthews KS, et al. (2009) Tetramer opening in LacI-mediated DNA looping. Proceedings of the National Academy of Sciences of the United States of America. 106: 16627-32
Zhan H, Sun Z, Matthews KS. (2009) Functional impact of polar and acidic substitutions in the lactose repressor hydrophobic monomer.monomer interface with a buried lysine. Biochemistry. 48: 1305-14
Rutkauskas D, Vanzi F, Zhan H, et al. (2009) Single Molecule Measurements Of The Role Of Tetramer Opening In LacI-mediated DNA Looping Biophysical Journal. 96: 62a-63a
Zhan H, Taraban M, Trewhella J, et al. (2008) Subdividing repressor function: DNA binding affinity, selectivity, and allostery can be altered by amino acid substitution of nonconserved residues in a LacI/GalR homologue. Biochemistry. 47: 8058-69
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