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Biochemistry|April 10, 1990
Salt-dependent structure change and ion binding in cytochrome c studied by two-dimensional proton NMRY Feng, S W EnglanderBiochemistry|May 20, 1986
Allosteric sensitivity in hemoglobin at the alpha-subunit N-terminus studied by hydrogen exchangeJ Ray, S W EnglanderBiochemistry|March 11, 1986
Two-dimensional 1H NMR studies of cytochrome c: assignment of the N-terminal helixA J Wand, S W EnglanderBiophysical Journal|July 1, 1978
Sickle hemoglobin gelation. Reaction order and critical nucleus sizeM J Behe, S W EnglanderBiochemistry|September 24, 1985
Two-dimensional 1H NMR studies of cytochrome cA J Wand, S W EnglanderBiochemistry|April 7, 1987
Hydrogen-tritium exchange survey of allosteric effects in hemoglobinJ J Englander, S W EnglanderBiochemistry|April 9, 1985
Internal protein motions, concentrated glycerol, and hydrogen exchange studied in myoglobinD B Calhoun, S W EnglanderCurrent Opinion in Biotechnology|August 1, 1996
Protein complexes studied by NMR spectroscopyA J Wand, S W EnglanderTrends in Biochemical Sciences|December 1, 1994
How much is a stabilizing bond worth?K A Sharp, S W EnglanderBiochemistry|September 22, 1987
Main-chain-directed strategy for the assignment of 1H NMR spectra of proteinsS W Englander, A J WandPageof 15