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Trends in Biochemical Sciences|November 1, 1990
Nucleation in protein folding--confusion of structure and processD B WetlauferProceedings of the National Academy of Sciences of the United States of America|March 1, 1973
Nucleation, rapid folding, and globular intrachain regions in proteinsD B WetlauferProtein Science : a Publication of the Protein Society|August 1, 1995
Control of aggregation in protein refolding: a variety of surfactants promote renaturation of carbonic anhydrase IID B Wetlaufer, Y XieProtein Science : a Publication of the Protein Society|March 1, 1996
Control of aggregation in protein refolding: the temperature-leap tacticY Xie, D B WetlauferJournal of Chromatography|February 17, 1989
Use of the surfactant 3-(3-cholamidopropyl)-dimethyl-ammoniopropane sulfonate in hydrophobic interaction chromatography of proteinsJ J Buckley, D B WetlauferJournal of Chromatography|March 14, 1986
Relationship between isocratic and gradient retention times in the high-performance ion-exchange chromatography of proteins. Theory and experimentE S Parente, D B WetlauferJournal of Chromatography|November 30, 1984
Effects of urea-thermal denaturation on the high-performance cation-exchange chromatography of alpha-chymotrypsinogen-AE S Parente, D B WetlauferJournal of Chromatography|April 24, 1984
Influence of urea on the high-performance cation-exchange chromatography of hen egg white lysozymeE S Parente, D B WetlauferProceedings of the National Academy of Sciences of the United States of America|May 1, 1971
A new basis for interpreting the circular dichroic spectra of proteinsV P Saxena, D B WetlauferPageof 6