C Ho

Direct measurement of the pK values of an alkaline Bohr group in human hemoglobin.

J. J. Breen, J J Breen, C. Ho, 1973, Proceedings of the National Academy of Sciences of the United States of America.

Influence of globin structure on the state of the heme. 3. Changes in heme spectra accompanying allosteric transitions in methemoglobin and their implications for heme-heme interaction.

J E Ladner, M. Perutz, C. Ho, 1974, Biochemistry.

The effects of phospholipid unsaturation and alcohol perturbation at the protein/lipid interface probed using fluorophore lifetime heterogeneity.

M. B. Kelly, C. Ho, C. Stubbs, 1994, Biochimica et biophysica acta.

Influence of globin structure on the state of the heme. I. Human deoxyhemoglobin.

J E Ladner, M. Perutz, C. Ho, 1974, Biochemistry.

A test of the role of the proximal histidines in the Perutz model for cooperativity in haemoglobin

F. Dahlquist, D. Barrick, V. Simplaceanu, 1997, Nature Structural Biology.

Contributions of asparagine at alpha 97 to the cooperative oxygenation process of hemoglobin.

C Ho, M F Tam, H W Kim, 1996, Biochemistry.

Roles of the beta 146 histidyl residue in the molecular basis of the Bohr effect of hemoglobin: a proton nuclear magnetic resonance study.

C. Ho, N. T. Ho, J. Mace, 1991, Biochemistry.