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Journal of Molecular Biology|March 19, 1999
Conformational analysis of a set of peptides corresponding to the entire primary sequence of the N-terminal domain of the ribosomal protein L9: evidence for stable native-like secondary structure in the unfolded stateD L Luisi, W J Wu, D P RaleighMagnetic Resonance in Medicine|May 1, 1992
Phosphorus-31 magnetic resonance imaging of hydroxyapatite: a model for bone imagingJ L Ackerman, D P Raleigh, M J GlimcherAnalytical Biochemistry|January 6, 2001
Synthesis and purification of amyloidogenic peptidesM R Nilsson, L L Nguyen, D P RaleighProteins|December 19, 2000
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-lactalbuminS J Demarest, J C Horng, D P RaleighThe Journal of Allergy and Clinical Immunology|March 9, 1999
Ideal pharmacotherapy for allergic rhinitisS SpectorThe Journal of Asthma : Official Journal of the Association for the Care of Asthma|September 13, 2000
Noncompliance with asthma therapy--are there solutions?S SpectorAllergie Et Immunologie|April 1, 1996
Bronchial inhalation challenge procedures with allergens and other bronchoconstrictor substancesS SpectorBiochemistry|April 14, 1999
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 interactionsB Kuhlman, D L Luisi, P Young, et al.Pageof 26