Ching-Hsuan Tsai

Enzymatic synthesis of DNA on glycerol nucleic acid templates without stable duplex formation between product and template

J. Szostak, Jack W Szostak, Ching-Hsuan Tsai, 2007, Proceedings of the National Academy of Sciences.

Hemoglobin site-mutants reveal dynamical role of interhelical H-bonds in the allosteric pathway: time-resolved UV resonance Raman evidence for intra-dimer coupling.

A. Pevsner, C. Ho, G. Mclendon, 2004, Journal of molecular biology.

Conjugation of Multiple Copies of Polyethylene Glycol to Hemoglobin Facilitated Through Thiolation: Influence on Hemoglobin Structure and Function

C. Ho, B. Manjula, K. Perumalsamy, 2005, The protein journal.

Hemoglobin Einstein: Semisynthetic deletion in the B‐helix of the α‐chain

C. Ho, B. Manjula, M. Prabhakaran, 2004 .

Site mutations disrupt inter-helical H-bonds (α14W–α67T and β15W–β72S) involved in kinetic steps in the hemoglobin R→T transition without altering the free energies of oxygenation

C. Ho, V. Simplaceanu, N. T. Ho, 2002 .

Recombinant hemoglobins with low oxygen affinity and high cooperativity.

C. Ho, Ching-Hsuan Tsai, 2002, Biophysical chemistry.

Enzymatic Primer-Extension with Glycerol-Nucleoside Triphosphates on DNA Templates

J. Szostak, Xin Cai, L. McLaughlin, 2009, PloS one.