Publications
Since joining TAMU (*corresponding author)
Heterogeneous and Allosteric Role of Surface Hydration for Protein-Ligand Binding. Shi J, Cho JH, Hwang W. J Chem Theory Comput. 2023
Energy landscape reshaped by strain-specific mutations underlies epistasis in NS1 evolution of influenza A virus. Kim I, Dubrow A, Zuniga B, Zhao B, Sherer N, Bastiray A, Li P, *Cho JH. Nature Communications, 2022, 13, 5775
Suppressing nonspecific binding in biolayer interferometry experiments for weak ligand-analyte interactions. Dubrow A, Zuniga B, Topo E, *Cho JH. ACS Omega, 2022, 7, 9206-9211
Understanding the Binding Transition State After the Conformational Selection Step: The Second Half of the Molecular Recognition Process Between NS1 of the 1918 Influenza Virus and Host p85β. Dubrow A, Kim I, Topo E, *Cho JH. Front Mol Biosci., 2021, 8:716477
Entropy hotspots for the binding of intrinsically disordered ligands to a receptor domain. Shi J, Shen Q, *Cho JH, *Hwang W. Biophys J, 2020, 118, 2502-2512
Molecular basis of the ternary interaction between NS1 of the 1918 influenza A virus, PI3K, and CRK. Dubrow A, Lin S, Savage N, Shen Q, *Cho JH. Viruses, 2020, 12, 338
Molecular recognition of a host protein by NS1 of pandemic and seasonal influenza A viruses. *Cho JH, Zhao B, Shi J, Savage N, Shen Q, Byrnes J, Yan L, Hwang W, Li P. Proc. Natl. Acad. Sci., 2020, 117, 6550-6558
The structure and conformational plasticity of the nonstructural protein 1 of the 1918 influenza A virus. Shen Q, *Cho JH. Biochem Biophys Res Commun, 2019, 518, 178-182
Molecular mechanisms of tight binding through fuzzy interactions. Shen Q, Shi J, Zeng D, Zhao B, Li P, *Hwang W, *Cho JH. Biophys. J. 2018, 114, 1313-1320.
Structure-guided design of a potent peptide-inhibitor targeting the interaction between CRK and ABL kinase. Shen Q, Bhatt VS, Krieger I, Sacchettini JC, *Cho JH. MedChemComm, 2018, 9, 519-524.
The molecular mechanisms underlying the hijack of host proteins by the 1918 Spanish influenza virus. Shen Q, Zeng D, Zhao B, Bhatt VS, Li P, *Cho JH. ACS Chemical Biology, 2017, 12, 1199-1203
The N-terminal domain of ribosomal protein L9 folds via a diffuse and delocalized transition state. Sato S, Cho JH (Co-first author), Peran I, Soydaner-Azeloglu RG, Raleigh DP, Biophysical Journal, 2017, 112, 1797-1806
Thermodynamic contribution of backbone conformational entropy in the binding between SH3 domain and proline-rich motif. Zeng D., Shen, Q., *Cho JH, Biochem Biophys Res Commun, 2017, 484, 21-26
Kinetic insights into the binding mechanism between the nSH3 domain of CrkII and proline-rich motifs in cAbl. Zeng, D., Bhatt, V.S., Shen, Q., *Cho JH. Biophysical Journal, 2016, 111, 1843-1853
Binding mechanism of the N-terminal SH3 domain of CrkII and proline-rich motifs in cAbl. Bhatt, V.S., Zeng, D., Krieger, I., Sacchettini, J.C., *Cho JH. Biophysical Journal, 2016, 110, 2630-2641
Energetically Significant, Non-Native, Cooperative Interactions Within an Unfolded Protein. Cho JH, Meng W, Sato S, Kim EY, Schindelin, H and *Raleigh DP. Proc. Natl. Acad. Sci., 2014, 111, 12079-12084
Side chain dynamics of carboxyl and carbonyl groups in the catalytic function of Escherichia coli ribonulcease H. Stafford KA, Ferrage F, *Cho JH (Co-Corresponding Author), *Palmer AG. J. Am. Chem. Soc. 2013, 135, 18024-18027
Before joining TAMU
Tuning protein autoinhibition by domain destabilization. Cho JH, Muralidharan V, Vila-Perello M, Raleigh DP, Muir TW, Palmer AG. Nat. Struct. Mol. Biol. 2011, 18, 550-555.
Phi-value analysis for ultrafast folding proteins by NMR relaxation dispersion. Cho JH, O'Connell N, Raleigh DP, Palmer AG. J Am Chem Soc. 2010, 132, 450-501.
Protein side-chain dynamics and residual conformational entropy. Trbovic N, Cho JH, Abel R, Friesner RA, Rance M, Palmer AG., J Am Chem Soc. 2009, 131, 615-622.
Experimental characterization of the denatured state ensemble of proteins. Cho JH, Raleigh DP. Methods Mol. Biol., 2009, 490, 339-351.
Temperature-dependent Hammond behavior in a protein-folding reaction: analysis of transition-state movement and ground-state effects. Taskent H, Cho JH, Raleigh DP. J. Mol. Biol., 2008, 378, 699-706.
Electrostatic interactions in the denatured state ensemble: their effect upon protein folding and protein stability. Cho JH, Sato S, Horng JC, Anil B, Raleigh DP. Arch Biochem Biophys. 2008, 469, 20-28.
Ionic-strength-dependent effects in protein folding: analysis of rate equilibrium free-energy relationships and their interpretation. Song B, Cho JH, Raleigh DP. Biochemistry. 2007, 46, 14206-14214.
Rational design, structural and thermodynamic characterization of a hyperstable variant of the villin headpiece helical subdomain. Bi Y, Cho JH, Kim EY, Shan B, Schindelin H, Raleigh DP. Biochemistr,. 2007, 46, 7497-7505
Mutational analysis of the folding transition state of the C-terminal domain of ribosomal protein L9: A protein with an unusual beta-sheet topology. Li Y, Gupta R, Cho JH, Raleigh DP. Biochemistry, 2007, 46, 1013-1021.
Denatured state effects and the origin of nonclassical Phi-values in protein folding. Cho JH, Raleigh DP. J. Am. Chem. Soc. 2006, 128, 16492-16493.
The unfolded state of the N-terminal domain of ribosomal protein L9 is compact in the absence of denaturant. Burcu A, Li Y, Cho JH, Raleigh DP. Biochemistry. 2006, 45, 10110-10116.
Solution structure and folding characteristics of the C-terminal SH3 domain of c-Crk-2. Muralidharan V, Dutta K. Cho JH, Vila-Perello M, Raleigh DP, Cowburn D, Muir TW. Biochemistry. 2006, 45, 9228-9237.
Characterization of the heparin binding site in the N-terminus of human pro-islet amyloid polypeptide: Implications for amyloid formation. Abedini A, Tracz SM, Cho JH, Raleigh DP. Biochemistry. 2006, 45, 10110-10116.
Electrostatic interactions in the denatured state and in the transition state for protein folding: Effects of denatured state interactions on the analysis of transition state structure. Cho JH, Raleigh DP. J. Mol. Biol. 2006, 360, 1094-1107.
Efficient high level expression of peptides and proteins as fusion proteins with the N-terminal domain of L9: Application to the villin headpiece helical subdomain. Bi Y, Tang Y, Raleigh DP, Cho JH. (co-corresponding author) Protein Expr Purif. 2006, 47, 16284-16291.
Fine structure analysis of a protein folding transition state: Distinguishing between hydrophobic stabilization and specific packing. Anil B, Sato S, Cho JH, Raleigh DP. J. Mol. Biol. 2005, 354, 693-705.
Mutational analysis demonstrates that specific electrostatic interactions can play a key role in the denatured state ensemble of proteins. Cho JH, Raleigh DP. J. Mol. Biol. 2005, 174-85
Analysis of the pH-dependent folding and stability of histidine point mutants allows characterization of the denatured state and transition state for protein folding. Horng JC, Cho JH, Raleigh DP. J. Mol. Biol. 2005, 345,163-73.
Domain-specific incorporation of noninvasive optical probes into recombinant proteins. Muralidharan V, Cho JH, Trester-Zedlitz M, Kowalik L, Chait BT, Raleigh DP, Muir TW. J. Am. Chem. Soc. 2004,126, 14004-12.
Thermodynamics and kinetics of non-native interactions in protein folding: A single point mutant significantly stabilizes the N-terminal domain of L9 by modulating non-native interactions in the denatured state. Cho JH, Sato S, Raleigh DP. J. Mol. Biol. 2004, 827-37
Insight Into the stereochemistry in the inhibition of Carboxypeptidase A with N-(Hydroxyaminocarbonyl)Phenylalanine: Binding modes of an enantiomeric pair of the inhibitor to Carboxypeptidase A. Cho JH, Kim DH, Chung SJ, Ha NC, Oh BH, Yong Choi K. Bioorg Med Chem. 2002, 10, 2015-22.
The role of Tyr248 probed by mutant bovine Carboxypeptidase A: Insight into the catalytic mechanism of Carboxypeptidase A. Cho JH, Kim DH, Lee KJ, Kim DH, Choi KY. Biochemistry. 2001, 40, 10197-203.
Equilibrium and kinetic analysis of folding of ketosteroid isomerase from Comamonas Testosteroni. Kim DH, Jang DS, Nam GH, Yun S, Cho JH, Choi G, Lee HC, Choi KY. Biochemistry. 2000, 39, 13084-92.
Understanding the Binding Transition State After the Conformational Selection Step: The Second Half of the Molecular Recognition Process Between NS1 of the 1918 Influenza Virus and Host p85β.
Since joining TAMU (*corresponding author)
Heterogeneous and Allosteric Role of Surface Hydration for Protein-Ligand Binding. Shi J, Cho JH, Hwang W. J Chem Theory Comput. 2023
Energy landscape reshaped by strain-specific mutations underlies epistasis in NS1 evolution of influenza A virus. Kim I, Dubrow A, Zuniga B, Zhao B, Sherer N, Bastiray A, Li P, *Cho JH. Nature Communications, 2022, 13, 5775
Suppressing nonspecific binding in biolayer interferometry experiments for weak ligand-analyte interactions. Dubrow A, Zuniga B, Topo E, *Cho JH. ACS Omega, 2022, 7, 9206-9211
Understanding the Binding Transition State After the Conformational Selection Step: The Second Half of the Molecular Recognition Process Between NS1 of the 1918 Influenza Virus and Host p85β. Dubrow A, Kim I, Topo E, *Cho JH. Front Mol Biosci., 2021, 8:716477
Entropy hotspots for the binding of intrinsically disordered ligands to a receptor domain. Shi J, Shen Q, *Cho JH, *Hwang W. Biophys J, 2020, 118, 2502-2512
Molecular basis of the ternary interaction between NS1 of the 1918 influenza A virus, PI3K, and CRK. Dubrow A, Lin S, Savage N, Shen Q, *Cho JH. Viruses, 2020, 12, 338
Molecular recognition of a host protein by NS1 of pandemic and seasonal influenza A viruses. *Cho JH, Zhao B, Shi J, Savage N, Shen Q, Byrnes J, Yan L, Hwang W, Li P. Proc. Natl. Acad. Sci., 2020, 117, 6550-6558
The structure and conformational plasticity of the nonstructural protein 1 of the 1918 influenza A virus. Shen Q, *Cho JH. Biochem Biophys Res Commun, 2019, 518, 178-182
Molecular mechanisms of tight binding through fuzzy interactions. Shen Q, Shi J, Zeng D, Zhao B, Li P, *Hwang W, *Cho JH. Biophys. J. 2018, 114, 1313-1320.
Structure-guided design of a potent peptide-inhibitor targeting the interaction between CRK and ABL kinase. Shen Q, Bhatt VS, Krieger I, Sacchettini JC, *Cho JH. MedChemComm, 2018, 9, 519-524.
The molecular mechanisms underlying the hijack of host proteins by the 1918 Spanish influenza virus. Shen Q, Zeng D, Zhao B, Bhatt VS, Li P, *Cho JH. ACS Chemical Biology, 2017, 12, 1199-1203
The N-terminal domain of ribosomal protein L9 folds via a diffuse and delocalized transition state. Sato S, Cho JH (Co-first author), Peran I, Soydaner-Azeloglu RG, Raleigh DP, Biophysical Journal, 2017, 112, 1797-1806
Thermodynamic contribution of backbone conformational entropy in the binding between SH3 domain and proline-rich motif. Zeng D., Shen, Q., *Cho JH, Biochem Biophys Res Commun, 2017, 484, 21-26
Kinetic insights into the binding mechanism between the nSH3 domain of CrkII and proline-rich motifs in cAbl. Zeng, D., Bhatt, V.S., Shen, Q., *Cho JH. Biophysical Journal, 2016, 111, 1843-1853
Binding mechanism of the N-terminal SH3 domain of CrkII and proline-rich motifs in cAbl. Bhatt, V.S., Zeng, D., Krieger, I., Sacchettini, J.C., *Cho JH. Biophysical Journal, 2016, 110, 2630-2641
Energetically Significant, Non-Native, Cooperative Interactions Within an Unfolded Protein. Cho JH, Meng W, Sato S, Kim EY, Schindelin, H and *Raleigh DP. Proc. Natl. Acad. Sci., 2014, 111, 12079-12084
Side chain dynamics of carboxyl and carbonyl groups in the catalytic function of Escherichia coli ribonulcease H. Stafford KA, Ferrage F, *Cho JH (Co-Corresponding Author), *Palmer AG. J. Am. Chem. Soc. 2013, 135, 18024-18027
Before joining TAMU
Tuning protein autoinhibition by domain destabilization. Cho JH, Muralidharan V, Vila-Perello M, Raleigh DP, Muir TW, Palmer AG. Nat. Struct. Mol. Biol. 2011, 18, 550-555.
Phi-value analysis for ultrafast folding proteins by NMR relaxation dispersion. Cho JH, O'Connell N, Raleigh DP, Palmer AG. J Am Chem Soc. 2010, 132, 450-501.
Protein side-chain dynamics and residual conformational entropy. Trbovic N, Cho JH, Abel R, Friesner RA, Rance M, Palmer AG., J Am Chem Soc. 2009, 131, 615-622.
Experimental characterization of the denatured state ensemble of proteins. Cho JH, Raleigh DP. Methods Mol. Biol., 2009, 490, 339-351.
Temperature-dependent Hammond behavior in a protein-folding reaction: analysis of transition-state movement and ground-state effects. Taskent H, Cho JH, Raleigh DP. J. Mol. Biol., 2008, 378, 699-706.
Electrostatic interactions in the denatured state ensemble: their effect upon protein folding and protein stability. Cho JH, Sato S, Horng JC, Anil B, Raleigh DP. Arch Biochem Biophys. 2008, 469, 20-28.
Ionic-strength-dependent effects in protein folding: analysis of rate equilibrium free-energy relationships and their interpretation. Song B, Cho JH, Raleigh DP. Biochemistry. 2007, 46, 14206-14214.
Rational design, structural and thermodynamic characterization of a hyperstable variant of the villin headpiece helical subdomain. Bi Y, Cho JH, Kim EY, Shan B, Schindelin H, Raleigh DP. Biochemistr,. 2007, 46, 7497-7505
Mutational analysis of the folding transition state of the C-terminal domain of ribosomal protein L9: A protein with an unusual beta-sheet topology. Li Y, Gupta R, Cho JH, Raleigh DP. Biochemistry, 2007, 46, 1013-1021.
Denatured state effects and the origin of nonclassical Phi-values in protein folding. Cho JH, Raleigh DP. J. Am. Chem. Soc. 2006, 128, 16492-16493.
The unfolded state of the N-terminal domain of ribosomal protein L9 is compact in the absence of denaturant. Burcu A, Li Y, Cho JH, Raleigh DP. Biochemistry. 2006, 45, 10110-10116.
Solution structure and folding characteristics of the C-terminal SH3 domain of c-Crk-2. Muralidharan V, Dutta K. Cho JH, Vila-Perello M, Raleigh DP, Cowburn D, Muir TW. Biochemistry. 2006, 45, 9228-9237.
Characterization of the heparin binding site in the N-terminus of human pro-islet amyloid polypeptide: Implications for amyloid formation. Abedini A, Tracz SM, Cho JH, Raleigh DP. Biochemistry. 2006, 45, 10110-10116.
Electrostatic interactions in the denatured state and in the transition state for protein folding: Effects of denatured state interactions on the analysis of transition state structure. Cho JH, Raleigh DP. J. Mol. Biol. 2006, 360, 1094-1107.
Efficient high level expression of peptides and proteins as fusion proteins with the N-terminal domain of L9: Application to the villin headpiece helical subdomain. Bi Y, Tang Y, Raleigh DP, Cho JH. (co-corresponding author) Protein Expr Purif. 2006, 47, 16284-16291.
Fine structure analysis of a protein folding transition state: Distinguishing between hydrophobic stabilization and specific packing. Anil B, Sato S, Cho JH, Raleigh DP. J. Mol. Biol. 2005, 354, 693-705.
Mutational analysis demonstrates that specific electrostatic interactions can play a key role in the denatured state ensemble of proteins. Cho JH, Raleigh DP. J. Mol. Biol. 2005, 174-85
Analysis of the pH-dependent folding and stability of histidine point mutants allows characterization of the denatured state and transition state for protein folding. Horng JC, Cho JH, Raleigh DP. J. Mol. Biol. 2005, 345,163-73.
Domain-specific incorporation of noninvasive optical probes into recombinant proteins. Muralidharan V, Cho JH, Trester-Zedlitz M, Kowalik L, Chait BT, Raleigh DP, Muir TW. J. Am. Chem. Soc. 2004,126, 14004-12.
Thermodynamics and kinetics of non-native interactions in protein folding: A single point mutant significantly stabilizes the N-terminal domain of L9 by modulating non-native interactions in the denatured state. Cho JH, Sato S, Raleigh DP. J. Mol. Biol. 2004, 827-37
Insight Into the stereochemistry in the inhibition of Carboxypeptidase A with N-(Hydroxyaminocarbonyl)Phenylalanine: Binding modes of an enantiomeric pair of the inhibitor to Carboxypeptidase A. Cho JH, Kim DH, Chung SJ, Ha NC, Oh BH, Yong Choi K. Bioorg Med Chem. 2002, 10, 2015-22.
The role of Tyr248 probed by mutant bovine Carboxypeptidase A: Insight into the catalytic mechanism of Carboxypeptidase A. Cho JH, Kim DH, Lee KJ, Kim DH, Choi KY. Biochemistry. 2001, 40, 10197-203.
Equilibrium and kinetic analysis of folding of ketosteroid isomerase from Comamonas Testosteroni. Kim DH, Jang DS, Nam GH, Yun S, Cho JH, Choi G, Lee HC, Choi KY. Biochemistry. 2000, 39, 13084-92.
Understanding the Binding Transition State After the Conformational Selection Step: The Second Half of the Molecular Recognition Process Between NS1 of the 1918 Influenza Virus and Host p85β.