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Science (New York, N.Y.)|August 17, 1990
An antibody binding site on cytochrome c defined by hydrogen exchange and two-dimensional NMRY Paterson, S W Englander, H RoderNature|October 20, 1988
Structural characterization of folding intermediates in cytochrome c by H-exchange labelling and proton NMRH Roder, G A Elöve, S W EnglanderScience (New York, N.Y.)|April 30, 1999
Chaperonin function: folding by forced unfoldingM Shtilerman, G H Lorimer, S W EnglanderProteins|April 1, 1996
Molecular collapse: the rate-limiting step in two-state cytochrome c foldingT R Sosnick, L Mayne, S W EnglanderBiochemistry|December 9, 1980
Hydrogen--deuterium exchange analysis of ligand--macromolecule interactions: ethidium--deoxyribonucleic acid systemC Mandal, S W Englander, N R KallenbachBiophysical Journal|January 1, 1990
Assignment of paramagnetically shifted resonances in the 1H NMR spectrum of horse ferricytochrome cY Q Feng, H Roder, S W EnglanderJournal of Molecular Biology|June 20, 1988
Salt, phosphate and the Bohr effect at the hemoglobin beta chain C terminus studied by hydrogen exchangeG Louie, J J Englander, S W EnglanderBiochemistry|March 11, 1986
Two-dimensional 1H NMR studies of cytochrome c: hydrogen exchange in the N-terminal helixA J Wand, H Roder, S W EnglanderThe Journal of Biological Chemistry|July 25, 1982
Re-examination of rhodopsin structure by hydrogen exchangeJ J Englander, N W Downer, S W EnglanderProceedings of the National Academy of Sciences of the United States of America|September 1, 1983
Normal mode paths for hydrogen exchange in the peptide ferrichromeR P Sheridan, R M Levy, S W EnglanderPageof 105