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Science (New York, N.Y.)|May 1, 1987
On the prevalence of room-temperature protein phosphorescenceJ M Vanderkooi, D B Calhoun, S W EnglanderJournal of Molecular Biology|June 20, 1988
Allosteric energy at the hemoglobin beta chain C terminus studied by hydrogen exchangeG Louie, T Tran, J J Englander, et al.Current Opinion in Structural Biology|February 1, 1996
Mechanisms and uses of hydrogen exchangeS W Englander, T R Sosnick, J J Englander, et al.Journal of Molecular Biology|January 8, 1999
Energetic components of the allosteric machinery in hemoglobin measured by hydrogen exchangeJ J Englander, G Louie, R E McKinnie, et al.Biophysical Chemistry|April 16, 1996
Measurement of protein structure change in active muscle by hydrogen-tritium exchangeM E Rodgers, J J Englander, S W Englander, et al.Biochemistry|November 1, 1988
Quenching of room temperature protein phosphorescence by added small moleculesD B Calhoun, S W Englander, W W Wright, et al.Biochemistry|March 29, 1983
Penetration of dioxygen into proteins studied by quenching of phosphorescence and fluorescenceD B Calhoun, J M Vanderkooi, G V Woodrow, et al.Proteins|October 1, 1986
Protein fluorescence quenching by small molecules: protein penetration versus solvent exposureD B Calhoun, J M Vanderkooi, G R Holtom, et al.Methods in Enzymology|January 1, 1995
Thermodynamic parameters from hydrogen exchange measurementsY Bai, J J Englander, L Mayne, et al.Science (New York, N.Y.)|June 19, 1992
Hydrogen exchange measurement of the free energy of structural and allosteric change in hemoglobinS W Englander, J J Englander, R E McKinnie, et al.Pageof 16