Stephen J. Demarest, Ph.D.
Affiliations: | 2000 | Stony Brook University, Stony Brook, NY, United States |
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Sign in to add mentor| Daniel P. Raleigh | grad student | 2000 | SUNY Stony Brook | |
| (Structural and physical characterization of the molten globule state of human alpha-lactalbumin using peptide and protein chemistry.) | ||||
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| Houde D, Demarest SJ. (2011) Fine details of IGF-1R activation, inhibition, and asymmetry determined by associated hydrogen /deuterium-exchange and peptide mass mapping. Structure (London, England : 1993). 19: 890-900 |
| Demarest SJ, Salbato J, Elia M, et al. (2005) Structural characterization of the cell wall binding domains of Clostridium difficile toxins A and B; evidence that Ca2+ plays a role in toxin A cell surface association. Journal of Molecular Biology. 346: 1197-206 |
| Demarest SJ, Deechongkit S, Dyson HJ, et al. (2004) Packing, specificity, and mutability at the binding interface between the p160 coactivator and CREB-binding protein. Protein Science : a Publication of the Protein Society. 13: 203-10 |
| Demarest SJ, Rogers J, Hansen G. (2004) Optimization of the antibody C(H)3 domain by residue frequency analysis of IgG sequences. Journal of Molecular Biology. 335: 41-8 |
| Horng JC, Demarest SJ, Raleigh DP. (2003) pH-dependent stability of the human alpha-lactalbumin molten globule state: contrasting roles of the 6 - 120 disulfide and the beta-subdomain at low and neutral pH. Proteins. 52: 193-202 |
| Demarest SJ, Zhou SQ, Robblee J, et al. (2001) 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. Biochemistry. 40: 2138-47 |
| Demarest SJ, Horng JC, Raleigh DP. (2001) 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: 237-42 |
| Demarest SJ, Raleigh DP. (2000) 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: 189-96 |
| Moriarty DF, Demarest SJ, Robblee J, et al. (2000) Local interactions and the role of the 6-120 disulfide bond in alpha-lactalbumin: implications for formation of the molten globule state. Biochimica Et Biophysica Acta. 1476: 9-19 |
| Demarest SJ, Boice JA, Fairman R, et al. (1999) Defining the core structure of the alpha-lactalbumin molten globule state. Journal of Molecular Biology. 294: 213-21 |