Published in Proc Natl Acad Sci U S A on January 25, 2005
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Mechanism of fibril formation by a 39-residue peptide (PAPf39) from human prostatic acidic phosphatase. Biochemistry (2009) 1.09
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Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. J Mol Biol (2006) 1.02
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Computational design of the Fyn SH3 domain with increased stability through optimization of surface charge charge interactions. Protein Sci (2007) 1.01
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Total chemical synthesis and X-ray crystal structure of a protein diastereomer: [D-Gln 35]ubiquitin. Angew Chem Int Ed Engl (2005) 0.99
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How to improve nature: study of the electrostatic properties of the surface of alpha-lactalbumin. Protein Eng Des Sel (2005) 0.90
Conformational dynamics and structural plasticity play critical roles in the ubiquitin recognition of a UIM domain. J Mol Biol (2010) 0.89
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Conformational and thermodynamic properties of peptide binding to the human S100P protein. Protein Sci (2002) 0.89
Pathogenic serum amyloid A 1.1 shows a long oligomer-rich fibrillation lag phase contrary to the highly amyloidogenic non-pathogenic SAA2.2. J Biol Chem (2012) 0.89
Calorimetric evidence for a two-state unfolding of the beta-hairpin peptide trpzip4. J Am Chem Soc (2006) 0.88
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The role and specificity of the catalytic and regulatory cation-binding sites of the Na+-pumping NADH:quinone oxidoreductase from Vibrio cholerae. J Biol Chem (2011) 0.87
Isothermal titration calorimetry. Methods Mol Biol (2002) 0.87
Annexin I and annexin II N-terminal peptides binding to S100 protein family members: specificity and thermodynamic characterization. Biochemistry (2009) 0.87
Statistical analysis of protein structures suggests that buried ionizable residues in proteins are hydrogen bonded or form salt bridges. Proteins (2011) 0.87
Universal convergence of the specific volume changes of globular proteins upon unfolding. Biochemistry (2009) 0.87
A computational approach for the rational design of stable proteins and enzymes: optimization of surface charge-charge interactions. Methods Enzymol (2009) 0.86
Crystal and NMR structures of a Trp-cage mini-protein benchmark for computational fold prediction. Proc Natl Acad Sci U S A (2012) 0.86
Kinetic consequences of native state optimization of surface-exposed electrostatic interactions in the Fyn SH3 domain. Proteins (2011) 0.85
Effect of gold nanoparticle structure on the conformation and function of adsorbed proteins. Biomaterials (2012) 0.85
Protonation/deprotonation effects on the stability of the Trp-cage miniprotein. Phys Chem Chem Phys (2011) 0.84
Pressure perturbation calorimetry of unfolded proteins. J Phys Chem B (2010) 0.84
Serum amyloid A 2.2 refolds into a octameric oligomer that slowly converts to a more stable hexamer. Biochem Biophys Res Commun (2011) 0.84
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Elimination of the C-cap in ubiquitin - structure, dynamics and thermodynamic consequences. Biophys Chem (2006) 0.82
Modulation of quaternary structure of S100 proteins by calcium ions. Biophys Chem (2010) 0.82
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Experimental test of the thermodynamic model of protein cooperativity using temperature-induced unfolding of a Ubq-UIM fusion protein. Biochemistry (2010) 0.81
NMR structure of the Apo-S100P protein. J Biomol NMR (2004) 0.80
Investigation of protein binding affinity in multimodal chromatographic systems using a homologous protein library. J Chromatogr A (2009) 0.80
Investigation of protein binding affinity and preferred orientations in ion exchange systems using a homologous protein library. Biotechnol Bioeng (2009) 0.79
Structural characterization of semen coagulum-derived SEM1(86-107) amyloid fibrils that enhance HIV-1 infection. Biochemistry (2014) 0.79
Electrostatic contribution of surface charge residues to the stability of a thermophilic protein: benchmarking experimental and predicted pKa values. PLoS One (2012) 0.79
Use of pressure perturbation calorimetry to characterize the volumetric properties of proteins. Methods Enzymol (2009) 0.78
Noncharged amino acid residues at the solvent-exposed positions in the middle and at the C terminus of the alpha-helix have the same helical propensity. Protein Sci (2003) 0.78
Backtracking due to residual structure in the unfolded state changes the folding of the third fibronectin type III domain from tenascin-C. J Phys Chem B (2013) 0.78
Bacterial expression and purification of the amyloidogenic peptide PAPf39 for multidimensional NMR spectroscopy. Protein Expr Purif (2013) 0.78
The role of cross-chain ionic interactions for the stability of collagen model peptides. Biophys J (2013) 0.77
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Thermodynamic and kinetic analysis of peptides derived from CapZ, NDR, p53, HDM2, and HDM4 binding to human S100B. Biochemistry (2012) 0.77
Novel interactions of the TRTK12 peptide with S100 protein family members: specificity and thermodynamic characterization. Biochemistry (2013) 0.77
Equilibrium and kinetic studies of protein cooperativity using urea-induced folding/unfolding of a Ubq-UIM fusion protein. Biophys Chem (2011) 0.77
Molecular determinants of expansivity of native globular proteins: a pressure perturbation calorimetry study. J Phys Chem B (2014) 0.77
Investigation into the molecular and thermodynamic basis of protein interactions in multimodal chromatography using functionalized nanoparticles. Langmuir (2014) 0.76
Structural and thermodynamic characterization of the recognition of the S100-binding peptides TRTK12 and p53 by calmodulin. Protein Sci (2014) 0.75
Advances in the analysis of conformational transitions in peptides using differential scanning calorimetry. Methods Mol Biol (2007) 0.75
Molecular Determinants of Temperature Dependence of Protein Volume Change upon Unfolding. J Phys Chem B (2017) 0.75
Both helical propensity and side-chain hydrophobicity at a partially exposed site in alpha-helix contribute to the thermodynamic stability of ubiquitin. Proteins (2005) 0.75
Alterations of Nonconserved Residues Affect Protein Stability and Folding Dynamics through Charge-Charge Interactions. J Phys Chem B (2015) 0.75