B. García-Moreno E.

发表

Local conformational fluctuations can modulate the coupling between proton binding and global structural transitions in proteins.

Vincent J Hilser, V. Hilser, S. Whitten, 2005, Proceedings of the National Academy of Sciences of the United States of America.

Self‐guided Langevin dynamics study of regulatory interactions in NtrC

Bernard R Brooks, Ana Damjanović, B. Brooks, 2009, Proteins.

Structural interpretation of pH and salt-dependent processes in proteins with computational methods.

B. García-Moreno E., C. A. Fitch, Carolyn A Fitch, 2004, Methods in enzymology.

Distance dependence and salt sensitivity of pairwise, coulombic interactions in a protein

Kelly K. Lee, B. García-Moreno E., C. A. Fitch, 2002, Protein science : a publication of the Protein Society.

The pKa Cooperative: A collaborative effort to advance structure‐based calculations of pKa values and electrostatic effects in proteins

J. Nielsen, M. Gunner, B. García-Moreno E., 2011, Proteins.

High apparent dielectric constants in the interior of a protein reflect water penetration.

E. Lattman, A. Gittis, B. García-Moreno E., 2000, Biophysical journal.

A statistical thermodynamic model of the protein ensemble.

T. Oas, V. Hilser, S. Whitten, 2006, Chemical reviews.

Structural origins of high apparent dielectric constants experienced by ionizable groups in the hydrophobic core of a protein.

B. García-Moreno E., C. Castañeda, A. Majumdar, 2011, Journal of molecular biology.

High tolerance for ionizable residues in the hydrophobic interior of proteins

B. García-Moreno E., C. Castañeda, Daniel G. Isom, 2008, Proceedings of the National Academy of Sciences.

Experimental pK(a) values of buried residues: analysis with continuum methods and role of water penetration.

Eaton E Lattman, E. Lattman, Kelly K. Lee, 2002, Biophysical journal.

Charges in the hydrophobic interior of proteins

B. García-Moreno E., C. Castañeda, D. Isom, 2010, Proceedings of the National Academy of Sciences.

The pK(a) values of acidic and basic residues buried at the same internal location in a protein are governed by different factors.

B. García-Moreno E., M. Harms, C. Castañeda, 2009, Journal of molecular biology.

A buried lysine that titrates with a normal pKa: Role of conformational flexibility at the protein–water interface as a determinant of pKavalues

Ana Damjanović, B. García-Moreno E., M. Harms, 2008, Protein science : a publication of the Protein Society.

High apparent dielectric constant inside a protein reflects structural reorganization coupled to the ionization of an internal Asp.

M. Stahley, A. Gittis, B. García-Moreno E., 2007, Biophysical journal.

The role of hydrophobic microenvironments in modulating pKa shifts in proteins

I. Simon, E. Mehler, M. Fuxreiter, 2002, Proteins.

Stabilization of internal charges in a protein: water penetration or conformational change?

B. García-Moreno E., B. Halle, J. Schlessman, 2004, Biophysical journal.

Anomalous Properties of Lys Residues Buried in the Hydrophobic Interior of a Protein Revealed with 15N-Detect NMR Spectroscopy.

Emily M Grasso, B. García-Moreno E., J. Schlessman, 2018, The journal of physical chemistry letters.

Conformational Reorganization Coupled to the Ionization of Internal Lys Residues in Proteins.

B. García-Moreno E., A. Majumdar, Daniel E Richman, 2015, Biochemistry.

Role of flexibility and polarity as determinants of the hydration of internal cavities and pockets in proteins.

A. Garcia, B. García-Moreno E., A. Damjanovic, 2007, Biophysical journal.

Toward computational design of protein crystals with improved resolution

Jeffrey J. Gray, J. Jeliazkov, J. Berger, 2019, bioRxiv.

Probing the physical determinants of thermal expansion of folded proteins.

Mohammad M. Islam, B. García-Moreno E., C. Royer, 2013, The journal of physical chemistry. B.

Arginine: Its pKa value revisited

L. McIntosh, B. García-Moreno E., C. A. Fitch, 2015, Protein science : a publication of the Protein Society.

Structural plasticity of staphylococcal nuclease probed by perturbation with pressure and pH

B. García-Moreno E., C. Roumestand, C. Royer, 2011, Proteins.

Large shifts in pKa values of lysine residues buried inside a protein

B. García-Moreno E., C. Castañeda, Daniel G. Isom, 2011, Proceedings of the National Academy of Sciences.

Arginine residues at internal positions in a protein are always charged

B. García-Moreno E., M. Harms, J. Schlessman, 2011, Proceedings of the National Academy of Sciences.

Salt effects on ionization equilibria of histidines in myoglobin.

B. García-Moreno E., C. J. Sarkisian, Y. Kao, 2000, Biophysical journal.

Charges in Hydrophobic Environments: A Strategy for Identifying Alternative States in Proteins.

B. García-Moreno E., J. Schlessman, A. Majumdar, 2017, Biochemistry.

The origin of pH-dependent changes in m-values for the denaturant-induced unfolding of proteins.

V. Hilser, S. Whitten, B. García-Moreno E., 2001, Journal of molecular biology.

Cavities determine the pressure unfolding of proteins

Jose A. Caro, Julien Roche, Catherine A. Royer, 2012, Proceedings of the National Academy of Sciences.

Molecular mechanisms of pH‐driven conformational transitions of proteins: Insights from continuum electrostatics calculations of acid unfolding

V. Hilser, S. Whitten, B. García-Moreno E., 2006, Proteins.

pH dependence of conformational fluctuations of the protein backbone

B. García-Moreno E., A. Majumdar, Daniel E. Richman, 2014, Proteins.

Structural and thermodynamic consequences of burial of an artificial ion pair in the hydrophobic interior of a protein

B. García-Moreno E., C. Castañeda, J. Schlessman, 2014, Proceedings of the National Academy of Sciences.

Structural, energetic, and dynamic responses of the native state ensemble of staphylococcal nuclease to cavity‐creating mutations

A. Garcia, B. García-Moreno E., C. Roumestand, 2013, Proteins.

The properties of buried ion pairs are governed by the propensity of proteins to reorganize

B. García-Moreno E., J. Schlessman, A. Majumdar, 2020, bioRxiv.

Backbone relaxation coupled to the ionization of internal groups in proteins: a self-guided Langevin dynamics study.

Bernard R Brooks, Xiongwu Wu, Ana Damjanović, 2008, Biophysical journal.

Protein dielectric constants determined from NMR chemical shift perturbations.

Damien Farrell, Jens Erik Nielsen, Kaare Teilum, 2013, Journal of the American Chemical Society.

Salt‐induced stabilization of apoflavodoxin at neutral pH is mediated through cation‐specific effects

B. García-Moreno E., J. Sancho, L. A. Campos, 2002, Protein science : a publication of the Protein Society.

Structure‐Based pKa Calculations Using Continuum Electrostatics Methods

B. García-Moreno E., C. A. Fitch, 2006, Current protocols in bioinformatics.

Crystallographic study of hydration of an internal cavity in engineered proteins with buried polar or ionizable groups.

A. Gittis, B. García-Moreno E., J. Schlessman, 2008, Biophysical journal.

Local Backbone Flexibility as a Determinant of the Apparent pKa Values of Buried Ionizable Groups in Proteins.

B. García-Moreno E., J. Schlessman, G. Ortega, 2017, Biochemistry.

Electrostatic effects in highly charged proteins: salt sensitivity of pKa values of histidines in staphylococcal nuclease.

Kelly K. Lee, B. García-Moreno E., C. A. Fitch, 2002, Biochemistry.

A Statistical Thermodynamic Model of the Protein Ensemble

T. Oas, V. Hilser, S. Whitten, 2006 .

Toward the computational design of protein crystals with improved resolution.

Jeffrey J. Gray, Jeffrey J Gray, Jeliazko R Jeliazkov, 2019, Acta crystallographica. Section D, Structural biology.

Electrostatic effects in unfolded staphylococcal nuclease

B. García-Moreno E., Nicholas C. Fitzkee, 2008, Protein science : a publication of the Protein Society.

Changes in stability upon charge reversal and neutralization substitution in staphylococcal nuclease are dominated by favorable electrostatic effects.

B. García-Moreno E., W. Stites, C. A. Fitch, 2003, Biochemistry.

pH dependence of stability of staphylococcal nuclease: evidence of substantial electrostatic interactions in the denatured state.

S. Whitten, B. García-Moreno E., B García-Moreno E, 2000, Biochemistry.