Publications

High-pressure NMR


2017

Roche J. Royer C.A, Roumestand C. (2017) Monitoring protein folding through high pressure NMR. Prog. Nucl. Magn. Reson. Spectrosc. 102-103: 15-31


2017

Luan M. Nguyen, Roche J.* (2017) High-pressure NMR techniques for the study of protein dynamics, folding and aggregation. J. Magn. Reson. 277: 179-185 *corresponding author


2016

Louis J.M, Roche J.* (2016) Evolution under drug pressure remodels the folding free-energy landscape of mature HIV-1 protease. J. Mol. Biol. 428: 2780-2792 *corresponding author


2015

Roche J, Louis J.M, Bax A, Best R. (2015) "Pressure-induced structural transition of mature HIV-1 Protease from a combined NMR/MD simulation approach". Proteins. 83: 2117-2123


2015

Tugarinov V, Libich D.A, Meyer V, Roche J, Clore G.M. (2015) "The energetics of a three-state protein folding system probed by high-pressure relaxation NMR from 1 to 2500 bar". Angew. Chem. Int. Ed. 54: 11157-11161


2013

Roche J, Dellarole M, Caro J.A, Norberto D.E, Garcia A.E, Garcia-Moreno B, Roumestand C, Royer C.A. (2013) "Effect of internal cavities on folding rates and routes revealed by real-time pressure-jump NMR spectroscopy". J. Am. Chem. Soc. 135: 14610-14618


2013

Roche J, Ying J, Maltsev A.S, Bax A. (2013) "Impact of hydrostatic pressure on an intrinsically disordered protein: a high-pressure NMR study of a-synuclein". Chembiochem. 14: 1754-1761


2012

Roche J, Dellarole M, Caro J.A, Guca E, Norberto D.E, Yang T, Garcia A.E, Roumestand C, Garcia-Moreno B, Royer C.A. (2012) "Remodeling of the folding free-energy landscape of staphylococcal nuclease by cavity- creating mutations". Biochemistry 51: 9535-9546


2012

Roche J, Caro J.A, Norberto D.E, Barthe P, Roumestand C, Schlessman J.L, Garcia A.E, Garcia-Moreno B, Royer C.A. (2012) "Cavities determine the pressure unfolding of proteins". Proc. Natl. Acad. Sci. USA. 109: 6945-6950


2011

Rouget J-B, Aksel T, Roche J, Saldana J.L, Garcia A.E, Barrick D, Royer C.A. (2011) "Size and sequence and the volume change of protein folding". J. Am. Chem. Soc. 133: 6020-6027


2011

Kitahara R, Hata K, Maeno A, Akasaka K, Chimenti M.S, Garcia-Moreno B, Schroer M.A, Jeworrek C, Tolan M, Winter R, Roche J, Roumestand C, Montet de Guillen K, Royer C.A. (2011) "Structural plasticity of staphylococcal nuclease probed by perturbation with pressure and pH". Proteins 79: 1293-1305


Scaffold proteins and disordered peptides involved in neurological diseases


2018

Baweja L, Roche J. (2018) Pushing the Limits of Structure-Based Models: Prediction of Non-globular Protein Folding and Fibrils Formation with Go-Model Simulations. J. Phys. Chem. B. DOI 10.1021/acs.jpcb.7b12129


2017

Shen Y, Roche J, Grishaev A, Bax A. (2017) Prediction of nearest neighbor effects on backbone torsion angles and NMR scalar coupling constants in disordered proteins. Protein Sci. 27: 146-158


2016

Roche J, Ying J, Shen Y, Torchia D.A, Bax A. (2016) ARTSY-J: convenient and precise measurement of 3 J HNHa couplings in medium-size proteins from TROSY-HSQC spectra. J. Magn. Reson. 268: 73-81


2016

Roche J, Shen Y, Jung Ho L, Jinfa Y, Bax A. (2016) Monomeric Ab 1-40 and Ab 1-42 peptides in solution adopt very similar ramachandran map distributions that closely resemble random coil. Biochemistry 55: 762-775


2015

Roche J, Ying J, Bax A. (2015) “Accurate measurement of 3 J HNHa couplings in small or disordered proteins from WATERGATE-optimized TROSY spectra”. J. Biomol. NMR 64: 1-7


2014

Maltsev A.S, Grishaev A, Roche J, Zasloff M, Bax A. (2014) "Improved cross validation of a static ubiquitin structure derived from high precision residual dipolar couplings measured in a drug-based liquid crystalline phase". J. Am. Chem. Soc. 136: 3752-3755


2013

Ying J, Roche J, Bax A. (2013) "Homonuclear decoupling for enhancing resolution and sensivity in NOE and RDC measurements of peptides and proteins". J. Magn. Reson. 241: 97-102


2013

Roche J, Ying J, Maltsev A.S, Bax A. (2013) "Impact of hydrostatic pressure on an intrinsically disordered protein: a high-pressure NMR study of a-synuclein". Chembiochem. 14: 1754-1761


Evolution of viral proteins


2016

Agniswamy J, Louis J.M, Roche J, Harrison R.W, Weber I.T (2016) Structural studies of a rationally selected multi-drug resistant HIV-1 protease reveal synergistic effect of distal mutations on flap dynamics. PLoS One. 11: e0168616


2016

Louis J.M, Baber J.L, Ghirlando R, Aniana A, Bax A, Roche J.* (2016) Insights into the conformation of the membrane proximal regions critical to the trimerization of the HIV-1 gp41 ectodomain bound to dodecyl phosphocholine micelles. PLoS One. 11: e0160597 *corresponding author


2016

Louis J.M, Roche J.* (2016) Evolution under drug pressure remodels the folding free-energy landscape of mature HIV-1 protease. J. Mol. Biol. 428: 2780-2792 *corresponding author


2015

Roche J, Louis J.M, Aniana A, Ghirlando R, Bax A. (2015) Complete dissociation of the HIV-1 gp41 ectodomain and membrane proximal regions upon phospholipid binding. J. Biolmol. NMR 61: 235-248


2014

Roche J, Louis J.M, Bax A. (2014) Conformation of inhibitor-free HIV-1 protease derived from NMR spectroscopy in a weakly oriented solution. Chembiochem. 16: 214-218 ©


2014

Louis J.M, Aniana A, Lohith K, Sayer J.M, Roche J, Bewley C.A, Clore G.M. (2014) Binding of HIV-1 gp41-directed neutralizing and non-neutralizing fragment antibody binding domain (Fab) and single chain variable fragment (ScFv) antibodies to the ectodomain of gp41 in the pre-hairpin and six-helix bundle conformations. PLoS One. 9: e1046833


2014

Roche J, Louis J.M, Grishaev A, Ying J, Bax A. (2014) "Dissociation of the trimeric gp41 ectodomain at the lipid-water interface suggests an active role in HIV-1 Env-mediated membrane fusion". Proc. Natl. Acad. Sci. USA. 111: 3425-3430


2013

Louis. J.M, Tozser J, Roche J, Matuz K, Aniana A, Sayer J.M. (2013) "Enhanced stability of monomer fold correlates with extreme drug resistance of HIV-1 Protease". Biochemistry 52: 7678-7688


Protein folding


2018

Baweja L, Roche J. (2018) Pushing the Limits of Structure-Based Models: Prediction of Non-globular Protein Folding and Fibrils Formation with Go-Model Simulations. J. Phys. Chem. B. DOI 10.1021/acs.jpcb.7b12129


2017

Roche J. Royer C.A, Roumestand C. (2017) Monitoring protein folding through high pressure NMR. Prog. Nucl. Magn. Reson. Spectrosc. 102-103: 15-31


2017

Luan M. Nguyen, Roche J.* (2017) High-pressure NMR techniques for the study of protein dynamics, folding and aggregation. J. Magn. Reson. 277: 179-185 *corresponding author


2015

Tugarinov V, Libich D.A, Meyer V, Roche J, Clore G.M. (2015) "The energetics of a three-state protein folding system probed by high-pressure relaxation NMR from 1 to 2500 bar". Angew. Chem. Int. Ed. 54: 11157-11161


2015

Dellarole M, Caro J.A, Roche J, Fossat M, Barthe P, Garcia-Moreno B, Royer C.A, Roumestand C (2015) "Evolutionarily conserved pattern of interactions in a protein revealed by local thermal expansion properties". J. Am. Chem. Soc. 137: 9354-9362


2013

Roche J, Dellarole M, Caro J.A, Norberto D.E, Garcia A.E, Garcia-Moreno B, Roumestand C, Royer C.A. (2013) "Effect of internal cavities on folding rates and routes revealed by real-time pressure-jump NMR spectroscopy". J. Am. Chem. Soc. 135: 14610-14618


2013

Dellarole M, Kobayashi K, Rouget J-B, Caro J.A, Roche J, Islam M.M, Garcia-Moreno B, Kuroda Y, Royer C.A. (2013) "Probing the physical determinants of thermal expansion of folded proteins". J. Phys. Chem. B. 117: 12742-12749


2013

Roche J, Caro J.A, Dellarole M, Guca E, Royer C.A, Garcia-Moreno B, Garcia A.E, Roumestand C. (2013) "Structural, energetic and dynamic responses of the native state ensemble of staphylococcal nuclease to cavity- creating mutations". Proteins 81: 1069-1080


2012

Roche J, Dellarole M, Caro J.A, Guca E, Norberto D.E, Yang T, Garcia A.E, Roumestand C, Garcia-Moreno B, Royer C.A. (2012) "Remodeling of the folding free-energy landscape of staphylococcal nuclease by cavity- creating mutations". Biochemistry 51: 9535-9546


2012

Roche J, Caro J.A, Norberto D.E, Barthe P, Roumestand C, Schlessman J.L, Garcia A.E, Garcia-Moreno B, Royer C.A. (2012) "Cavities determine the pressure unfolding of proteins". Proc. Natl. Acad. Sci. USA. 109: 6945-6950


2011

Rouget J-B, Aksel T, Roche J, Saldana J.L, Garcia A.E, Barrick D, Royer C.A. (2011) "Size and sequence and the volume change of protein folding". J. Am. Chem. Soc. 133: 6020-6027


2018


Baweja L, Roche J. (2018) Pushing the Limits of Structure-Based Models: Prediction of Non-globular Protein Folding and Fibrils Formation with Go-Model Simulations. J. Phys. Chem. B. DOI 10.1021/acs.jpcb.7b12129


2017


Shen Y, Roche J, Grishaev A, Bax A. (2017) Prediction of nearest neighbor effects on backbone torsion angles and NMR scalar coupling constants in disordered proteins. Protein Sci. 27: 146-158


Roche J. Royer C.A, Roumestand C. (2017) Monitoring protein folding through high pressure NMR. Prog. Nucl. Magn. Reson. Spectrosc. 102-103: 15-31


Luan M. Nguyen, Roche J.* (2017) High-pressure NMR techniques for the study of protein dynamics, folding and aggregation. J. Magn. Reson. 277: 179-185 *corresponding author


2016


Agniswamy J, Louis J.M, Roche J, Harrison R.W, Weber I.T (2016) Structural studies of a rationally selected multi-drug resistant HIV-1 protease reveal synergistic effect of distal mutations on flap dynamics. PLoS One. 11: e0168616


Louis J.M, Baber J.L, Ghirlando R, Aniana A, Bax A, Roche J.* (2016) Insights into the conformation of the membrane proximal regions critical to the trimerization of the HIV-1 gp41 ectodomain bound to dodecyl phosphocholine micelles. PLoS One. 11: e0160597 *corresponding author


Louis J.M, Roche J.* (2016) Evolution under drug pressure remodels the folding free-energy landscape of mature HIV-1 protease. J. Mol. Biol. 428: 2780-2792 *corresponding author


Roche J, Ying J, Shen Y, Torchia D.A, Bax A. (2016) ARTSY-J: convenient and precise measurement of 3 J HNHa couplings in medium-size proteins from TROSY-HSQC spectra. J. Magn. Reson. 268: 73-81


Roche J, Shen Y, Jung Ho L, Jinfa Y, Bax A. (2016) Monomeric Ab 1-40 and Ab 1-42 peptides in solution adopt very similar ramachandran map distributions that closely resemble random coil. Biochemistry 55: 762-775


2015


Roche J, Ying J, Bax A. (2015) “Accurate measurement of 3 J HNHa couplings in small or disordered proteins from WATERGATE-optimized TROSY spectra”. J. Biomol. NMR 64: 1-7


Roche J, Louis J.M, Bax A, Best R. (2015) "Pressure-induced structural transition of mature HIV-1 Protease from a combined NMR/MD simulation approach". Proteins. 83: 2117-2123


Tugarinov V, Libich D.A, Meyer V, Roche J, Clore G.M. (2015) "The energetics of a three-state protein folding system probed by high-pressure relaxation NMR from 1 to 2500 bar". Angew. Chem. Int. Ed. 54: 11157-11161


Dellarole M, Caro J.A, Roche J, Fossat M, Barthe P, Garcia-Moreno B, Royer C.A, Roumestand C (2015) "Evolutionarily conserved pattern of interactions in a protein revealed by local thermal expansion properties". J. Am. Chem. Soc. 137: 9354-9362


Roche J, Louis J.M, Aniana A, Ghirlando R, Bax A. (2015) Complete dissociation of the HIV-1 gp41 ectodomain and membrane proximal regions upon phospholipid binding. J. Biolmol. NMR 61: 235-248


2014


Roche J, Louis J.M, Bax A. (2014) Conformation of inhibitor-free HIV-1 protease derived from NMR spectroscopy in a weakly oriented solution. Chembiochem. 16: 214-218 ©


Louis J.M, Aniana A, Lohith K, Sayer J.M, Roche J, Bewley C.A, Clore G.M. (2014) Binding of HIV-1 gp41-directed neutralizing and non-neutralizing fragment antibody binding domain (Fab) and single chain variable fragment (ScFv) antibodies to the ectodomain of gp41 in the pre-hairpin and six-helix bundle conformations. PLoS One. 9: e1046833


Maltsev A.S, Grishaev A, Roche J, Zasloff M, Bax A. (2014) "Improved cross validation of a static ubiquitin structure derived from high precision residual dipolar couplings measured in a drug-based liquid crystalline phase". J. Am. Chem. Soc. 136: 3752-3755


Roche J, Louis J.M, Grishaev A, Ying J, Bax A. (2014) "Dissociation of the trimeric gp41 ectodomain at the lipid-water interface suggests an active role in HIV-1 Env-mediated membrane fusion". Proc. Natl. Acad. Sci. USA. 111: 3425-3430


2013


Ying J, Roche J, Bax A. (2013) "Homonuclear decoupling for enhancing resolution and sensivity in NOE and RDC measurements of peptides and proteins". J. Magn. Reson. 241: 97-102


Louis. J.M, Tozser J, Roche J, Matuz K, Aniana A, Sayer J.M. (2013) "Enhanced stability of monomer fold correlates with extreme drug resistance of HIV-1 Protease". Biochemistry 52: 7678-7688


Roche J, Dellarole M, Caro J.A, Norberto D.E, Garcia A.E, Garcia-Moreno B, Roumestand C, Royer C.A. (2013) "Effect of internal cavities on folding rates and routes revealed by real-time pressure-jump NMR spectroscopy". J. Am. Chem. Soc. 135: 14610-14618


Roche J, Ying J, Maltsev A.S, Bax A. (2013) "Impact of hydrostatic pressure on an intrinsically disordered protein: a high-pressure NMR study of a-synuclein". Chembiochem. 14: 1754-1761


Dellarole M, Kobayashi K, Rouget J-B, Caro J.A, Roche J, Islam M.M, Garcia-Moreno B, Kuroda Y, Royer C.A. (2013) "Probing the physical determinants of thermal expansion of folded proteins". J. Phys. Chem. B. 117: 12742-12749


Roche J, Caro J.A, Dellarole M, Guca E, Royer C.A, Garcia-Moreno B, Garcia A.E, Roumestand C. (2013) "Structural, energetic and dynamic responses of the native state ensemble of staphylococcal nuclease to cavity- creating mutations". Proteins 81: 1069-1080


2012


Roche J, Dellarole M, Caro J.A, Guca E, Norberto D.E, Yang T, Garcia A.E, Roumestand C, Garcia-Moreno B, Royer C.A. (2012) "Remodeling of the folding free-energy landscape of staphylococcal nuclease by cavity- creating mutations". Biochemistry 51: 9535-9546


Roche J, Caro J.A, Norberto D.E, Barthe P, Roumestand C, Schlessman J.L, Garcia A.E, Garcia-Moreno B, Royer C.A. (2012) "Cavities determine the pressure unfolding of proteins". Proc. Natl. Acad. Sci. USA. 109: 6945-6950


2011


Rouget J-B, Aksel T, Roche J, Saldana J.L, Garcia A.E, Barrick D, Royer C.A. (2011) "Size and sequence and the volume change of protein folding". J. Am. Chem. Soc. 133: 6020-6027


Kitahara R, Hata K, Maeno A, Akasaka K, Chimenti M.S, Garcia-Moreno B, Schroer M.A, Jeworrek C, Tolan M, Winter R, Roche J, Roumestand C, Montet de Guillen K, Royer C.A. (2011) "Structural plasticity of staphylococcal nuclease probed by perturbation with pressure and pH". Proteins 79: 1293-1305