D P Raleigh

pKa values and the pH dependent stability of the N-terminal domain of L9 as probes of electrostatic interactions in the denatured state. Differentiation between local and nonlocal interactions.

B. Kuhlman, D. Raleigh, P. Young, 1999, Biochemistry.

Global analysis of the effects of temperature and denaturant on the folding and unfolding kinetics of the N-terminal domain of the protein L9.

B. Kuhlman, D. Raleigh, D. Luisi, 1998, Journal of molecular biology.

Local interactions drive the formation of nonnative structure in the denatured state of human alpha-lactalbumin: a high resolution structural characterization of a peptide model in aqueous solution.

D. Raleigh, S. Demarest, D P Raleigh, 1999, Biochemistry.

Submillisecond folding of the peripheral subunit-binding domain.

D. Raleigh, S. Spector, D P Raleigh, 1999, Journal of molecular biology.

De novo design of helical bundles as models for understanding protein folding and function.

D. Raleigh, W. DeGrado, A. Lombardi, 2000, Accounts of chemical research.

Conformational analysis of peptide fragments derived from the peripheral subunit-binding domain from the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus: evidence for nonrandom structure in the unfolded state.

D. Raleigh, S. Spector, M. Rosconi, 1999, Biopolymers.

On the relationship between protein stability and folding kinetics: a comparative study of the N-terminal domains of RNase HI, E. coli and Bacillus stearothermophilus L9.

D. Raleigh, S. Sato, D P Raleigh, 2001, Journal of molecular biology.