Authors: Demarest, SJ Horng, JC Raleigh, DP

Citation: Sj. Demarest et al., A protein dissection study demonstrates that two specific hydrophobic clusters play a key role in stabilizing the core structure of the molten globule state of human alpha-lactalbumin, PROTEINS, 42(2), 2001, pp. 237-242

Authors: Demarest, SJ Zhou, SQ Robblee, J Fairman, R Chu, B Raleigh, DP

Citation: Sj. Demarest et al., A comparative study of peptide models of the alpha-domain of alpha-lactalbumin, lysozyme, and alpha-lactalbumin/lysozyme chimeras allows the elucidation of critical factors that contribute to the ability to form stable partially folded states, BIOCHEM, 40(7), 2001, pp. 2138-2147

Authors: Demarest, SJ Raleigh, DP

Citation: Sj. Demarest et Dp. Raleigh, Solution structure of a peptide model of a region important for the folding of alpha-lactalbumin provides evidence for the formation of nonnative structure in the denatured state, PROTEINS, 38(2), 2000, pp. 189-196

Authors: Moriarty, DF Demarest, SJ Robblee, J Fairman, R Raleigh, DP

Citation: Df. Moriarty et al., Local interactions and the role of the 6-120 disulfide bond in alpha-lactalbumin: implications for formation of the molten globule state, BBA-PROT ST, 1476(1), 2000, pp. 9-19

Authors: Demarest, SJ Boice, JA Fairman, R Raleigh, DP

Citation: Sj. Demarest et al., Defining the core structure of the alpha-lactalbumin molten globule state, J MOL BIOL, 294(1), 1999, pp. 213-221

Authors: Demarest, SJ Hua, YX Raleigh, DP

Citation: Sj. Demarest et al., 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, BIOCHEM, 38(22), 1999, pp. 7380-7387