Structure, Function, Folding, and Aggregation of a Neuroferritinopathy-Related Ferritin Variant. , Biochemistry, 58( 18), 2318- 2325, May. 2019, https://doi.org/10.1021/acs.biochem.8b01068 

β-strand twisting/bending in soluble and transmembrane β-barrel structures. , Proteins, ,   , Jul. 2018, https://doi.org/10.1002/prot.25576 

Optimization of Haemophilus influenzae adhesin transmembrane domain expression in Escherichia coli , Protein Expression and Purification, 145,  19- 24, May. 1, 2018, https://doi.org/10.1016/j.pep.2017.12.009 

Electrostatic Repulsion between Unique Arginine Residues Is Essential for the Efficient in Vitro Assembly of the Transmembrane Domain of a Trimeric Autotransporter , BIOCHEMISTRY, 56( 15), 2139- 2148, Apr. 2017, https://doi.org/10.1021/acs.biochem.6b01130 

Electrostatic Repulsion during Ferritin Assembly and Its Screening by Ions , BIOCHEMISTRY, 55( 3), 482- 488, Jan. 2016, https://doi.org/10.1021/acs.biochem.5b01197 

Ferritin Assembly Revisited: A Time-Resolved Small-Angle X-ray Scattering Study , BIOCHEMISTRY, 55( 2), 287- 293, Jan. 2016, https://doi.org/10.1021/acs.biochem.5b01152 

Role of electrostatic repulsion between unique arginine residues on the assembly of a trimeric autotransporter translocator domain , PROTEIN SCIENCE, 24,  89- 90, Oct. 2015,  

Role of a non-native alpha-helix in the folding of equine beta-lactoglobulin , PROTEIN SCIENCE, 24,  94- 94, Oct. 2015,  

Repulsion between net charges of subunits during ferritin assembly , PROTEIN SCIENCE, 24,  87- 88, Oct. 2015,  

A Physicochemical and Mutational Analysis of Intersubunit Interactions of Escherichia coli Ferritin A , BIOCHEMISTRY, 54( 40), 6243- 6251, Oct. 2015, https://doi.org/10.1021/acs.biochem.5b00723 

The origin of beta-strand bending in globular proteins , BMC STRUCTURAL BIOLOGY, 15,  21- , Oct. 2015, https://doi.org/10.1186/s12900-015-0048-y 

Effect of non-native helix destabilization on the folding of equine beta-lactoglobulin , JOURNAL OF BIOCHEMISTRY, 156( 5), 291- 297, Nov. 2014, https://doi.org/10.1093/jb/mvu043 

Local sequence of protein beta-strands influences twist and bend angles , PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS, 82( 7), 1484- 1493, Jul. 2014, https://doi.org/10.1002/prot.24518 

Relationship Between Chain Collapse and Secondary Structure Formation in a Partially Folded Protein , BIOPOLYMERS, 101( 6), 651- 658, Jun. 2014, https://doi.org/10.1002/bip.22433 

Delineation of Solution Burst-Phase Protein Folding Events by Encapsulating the Proteins in Silica Gels , BIOCHEMISTRY, 53( 23), 3858- 3866, Jun. 2014, https://doi.org/10.1021/bi5003647 

Dependence of alpha-helical and beta-sheet amino acid propensities on the overall protein fold type , BMC STRUCTURAL BIOLOGY, 12,  18- , Aug. 2012, https://doi.org/10.1186/1472-6807-12-18 

Important role of methionine 145 in dimerization of bovine beta-lactoglobulin , JOURNAL OF BIOCHEMISTRY, 151( 3), 329- 334, Mar. 2012, https://doi.org/10.1093/jb/mvr142 

A Native Disulfide Stabilizes Non-Native Helical Structures in Partially Folded States of Equine beta-Lactoglobulin , BIOCHEMISTRY, 50( 49), 10590- 10597, Dec. 2011, https://doi.org/10.1021/bi2013239 

Correction to the article "non-native α-helix formation is not necessary for folding of lipocalin: Comparison of burst-phase folding between tear lipocalin and β-lactoglobulin" (Proteins: Structute, Function and Bioformatics (2009) 76, (226-236)) , Proteins: Structure, Function and Bioinformatics, 77,  1015- , Nov. 25, 2009, https://doi.org/10.1002/prot.22593 

Fatty Acids Bound to Recombinant Tear Lipocalin and Their Role in Structural Stabilization , JOURNAL OF BIOCHEMISTRY, 146( 3), 343- 350, Sep. 2009, https://doi.org/10.1093/jb/mvp076 

Non-native alpha-helix formation is not necessary for folding of lipocalin: Comparison of burst-phase folding between tear lipocalin and beta-lactoglobulin , PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS, 76( 1), 226- 236, Jul. 2009, https://doi.org/10.1002/prot.22340 

OLIGAMI: OLIGomer Architecture and Molecular Interface , The Open Bioinformatics Journal, 2( 1), 50- 53, Sep. 2008,  

Chloride-ion concentration dependence of molecular dimension in the acid-denatured state of equine β-lactoglobulin , Journal of Applied Crystallography, 40,   , Apr. 1, 2007, https://doi.org/10.1107/S0021889807008278 

Interactions responsible for secondary structure formation during folding of equine beta-lactoglobulin , JOURNAL OF MOLECULAR BIOLOGY, 367( 4), 1205- 1214, Apr. 2007, https://doi.org/10.1016/j.jmb.2007.01.053 

Proline scanning mutagenesis reveals non-native fold in the molten globule state of equine beta-lactoglobulin , BIOCHEMISTRY, 45( 51), 15468- 15473, Dec. 2006, https://doi.org/10.1021/bi061420p 

Structural and thermodynamic consequences of removal of a conserved disulfide bond from equine beta-lactoglobulin , PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS, 63( 3), 595- 602, May. 2006, https://doi.org/10.1002/prot.20905 

Helical and expanded conformation of equine beta-lactoglobulin in the cold-denatured state , JOURNAL OF MOLECULAR BIOLOGY, 350( 2), 338- 348, Jul. 2005, https://doi.org/10.1016/j.jmb.2005.05.003 

A partially unfolded state of equine β-lactoglobulin at pH 8.7 , Protein Journal, 20,  131- 137, Dec. 1, 2001, https://doi.org/10.1023/A:1011029524100 

Folding-unfolding equilibrium and kinetics of equine beta-lactoglobulin: Equivalence between the equilibrium molten globule state and a burst-phase folding intermediate , BIOCHEMISTRY, 38( 14), 4455- 4463, Apr. 1999, https://doi.org/10.1021/bi982683p