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Items: 1 to 20 of 137


Conformational consequences of ionization of Lys, Asp, and Glu buried at position 66 in staphylococcal nuclease.

Karp DA, Stahley MR, García-Moreno B.

Biochemistry. 2010 May 18;49(19):4138-46. doi: 10.1021/bi902114m.


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

Chimenti MS, Castañeda CA, Majumdar A, García-Moreno E B.

J Mol Biol. 2011 Jan 14;405(2):361-77. doi: 10.1016/j.jmb.2010.10.001. Epub 2010 Nov 6.


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

Fitch CA, Karp DA, Lee KK, Stites WE, Lattman EE, García-Moreno E B.

Biophys J. 2002 Jun;82(6):3289-304.


Molecular determinants of the pKa values of Asp and Glu residues in staphylococcal nuclease.

Castañeda CA, Fitch CA, Majumdar A, Khangulov V, Schlessman JL, García-Moreno BE.

Proteins. 2009 Nov 15;77(3):570-88. doi: 10.1002/prot.22470.


A buried lysine that titrates with a normal pKa: role of conformational flexibility at the protein-water interface as a determinant of pKa values.

Harms MJ, Schlessman JL, Chimenti MS, Sue GR, Damjanović A, García-Moreno B.

Protein Sci. 2008 May;17(5):833-45. doi: 10.1110/ps.073397708. Epub 2008 Mar 27.


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

Karp DA, Gittis AG, Stahley MR, Fitch CA, Stites WE, García-Moreno E B.

Biophys J. 2007 Mar 15;92(6):2041-53. Epub 2006 Dec 15.


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

Robinson AC, Majumdar A, Schlessman JL, García-Moreno E B.

Biochemistry. 2017 Jan 10;56(1):212-218. doi: 10.1021/acs.biochem.6b00843. Epub 2016 Dec 23.


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

Isom DG, Castañeda CA, Cannon BR, García-Moreno B.

Proc Natl Acad Sci U S A. 2011 Mar 29;108(13):5260-5. doi: 10.1073/pnas.1010750108. Epub 2011 Mar 9.


Charges in the hydrophobic interior of proteins.

Isom DG, Castañeda CA, Cannon BR, Velu PD, García-Moreno E B.

Proc Natl Acad Sci U S A. 2010 Sep 14;107(37):16096-100. doi: 10.1073/pnas.1004213107. Epub 2010 Aug 26.


The high dielectric constant of staphylococcal nuclease is encoded in its structural architecture.

Goh GB, García-Moreno E B, Brooks CL 3rd.

J Am Chem Soc. 2011 Dec 21;133(50):20072-5. doi: 10.1021/ja2084866. Epub 2011 Nov 23.


Molecular dynamics study of water penetration in staphylococcal nuclease.

Damjanović A, García-Moreno B, Lattman EE, García AE.

Proteins. 2005 Aug 15;60(3):433-49.


Conformational relaxation and water penetration coupled to ionization of internal groups in proteins.

Damjanović A, Brooks BR, García-Moreno B.

J Phys Chem A. 2011 Apr 28;115(16):4042-53. doi: 10.1021/jp110373f. Epub 2011 Mar 23.


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

Harms MJ, Castañeda CA, Schlessman JL, Sue GR, Isom DG, Cannon BR, García-Moreno E B.

J Mol Biol. 2009 May 29;389(1):34-47. doi: 10.1016/j.jmb.2009.03.039. Epub 2009 Mar 24.


pH dependence of conformational fluctuations of the protein backbone.

Richman DE, Majumdar A, García-Moreno E B.

Proteins. 2014 Nov;82(11):3132-43. doi: 10.1002/prot.24673. Epub 2014 Sep 4.


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

Richman DE, Majumdar A, García-Moreno E B.

Biochemistry. 2015 Sep 29;54(38):5888-97. doi: 10.1021/acs.biochem.5b00522. Epub 2015 Sep 16.


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

Dwyer JJ, Gittis AG, Karp DA, Lattman EE, Spencer DS, Stites WE, García-Moreno E B.

Biophys J. 2000 Sep;79(3):1610-20.


Structural reorganization triggered by charging of Lys residues in the hydrophobic interior of a protein.

Chimenti MS, Khangulov VS, Robinson AC, Heroux A, Majumdar A, Schlessman JL, García-Moreno B.

Structure. 2012 Jun 6;20(6):1071-85. doi: 10.1016/j.str.2012.03.023. Epub 2012 May 25.


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

Damjanović A, Wu X, García-Moreno E B, Brooks BR.

Biophys J. 2008 Nov 1;95(9):4091-101. doi: 10.1529/biophysj.108.130906. Epub 2008 Jul 18.


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

Kitahara R, Hata K, Maeno A, Akasaka K, Chimenti MS, Garcia-Moreno E B, Schroer MA, Jeworrek C, Tolan M, Winter R, Roche J, Roumestand C, Montet de Guillen K, Royer CA.

Proteins. 2011 Apr;79(4):1293-305. doi: 10.1002/prot.22966. Epub 2011 Jan 20.


X-ray and thermodynamic studies of staphylococcal nuclease variants I92E and I92K: insights into polarity of the protein interior.

Nguyen DM, Leila Reynald R, Gittis AG, Lattman EE.

J Mol Biol. 2004 Aug 6;341(2):565-74.


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