S. L. Flaugh

Effects of macromolecular crowding on the intrinsically disordered proteins c-Fos and p27(Kip1).

K. Lumb, S. L. Flaugh, 2001, Biomacromolecules.

Contributions of hydrophobic domain interface interactions to the folding and stability of human γD‐crystallin

J. King, S. L. Flaugh, M. Kosinski-Collins, 2005, Protein science : a publication of the Protein Society.

Glutamine Deamidation Destabilizes Human γD-Crystallin and Lowers the Kinetic Barrier to Unfolding*

J. King, S. L. Flaugh, I. A. Mills, 2006, Journal of Biological Chemistry.

Probing folding and fluorescence quenching in human γD crystallin Greek key domains using triple tryptophan mutant proteins

J. King, S. L. Flaugh, M. Kosinski-Collins, 2004, Protein science : a publication of the Protein Society.

Folding, stability and aggregation of the long-lived eye lens protein human gamma D crystallin

S. L. Flaugh, 2006 .

Mechanism of the highly efficient quenching of tryptophan fluorescence in human gammaD-crystallin.

J. King, P. Callis, S. L. Flaugh, 2006, Biochemistry.

Folding and stability of the isolated Greek key domains of the long‐lived human lens proteins γD‐crystallin and γS‐crystallin

J. King, S. L. Flaugh, M. Kosinski-Collins, 2007, Protein science : a publication of the Protein Society.

Interdomain side‐chain interactions in human γD crystallin influencing folding and stability

Melissa S Kosinski-Collins, J. King, S. L. Flaugh, 2005, Protein science : a publication of the Protein Society.

Folding and stability of the isolated Greek key domains of the long-lived human lens proteins gammaD-crystallin and gammaS-crystallin.

J. King, S. L. Flaugh, M. Kosinski-Collins, 2007, Protein science : a publication of the Protein Society.