The University of Texas Health Science Center at Houston
Colorful photo of a DNA model
The Brown Foundation Institute of Molecular Medicine
for the Prevention of Human Diseases

Rowen J.-Y. Chang, Ph.D.

Professor and Director, Center for Protein Chemistry
phone 713.500.2458; fax: 713.500.2447
Rowen.Chang@uth.tmc.edu

Photo of Dr. Rowen J.-Y. Chang

Dr. Chang obtained his MS degree from the National Taiwan University at Taipei in 1974 and his Ph.D. from the Australian National University at Canberra in 1977. He did his postdoctoral training from 1978 to 1980 at Max-Planck Institute at Berlin (protein chemistry) and Mayo Clinic at Rochester (Immunochemistry).

In 1981, Dr. Chang joined Ciba-Geigy at Basel, Switzerland where he was responsible for the protein chemistry laboratory. In July 1998, he joined the Institute of Molecular Medicine, University of Texas Health Science Center at Houston, as Professor and Director of the Center for Protein Chemistry.

RECENT PUBLICATIONS

Lu, B.-Y., and  Chang, J.-Y. (2007) Arch. Biochem. Biophys.  460, 75-84.
A 3-Disulfide Mutant of Mouse Prion Protein: EXPRESSION, OXIDATIVE FOLDING, REDUCTIVE UNFOLDING, CONFORMATIONAL STABILITY, AGGREGATION AND ISOMERIZATION.

Lin, C.-J. and  Chang, J.-Y. (2007)  Biochemistry  46, 3925-3932.
Pathway of Oxidative Folding of Bovine a-Interferon: PREDOMINANCE OF NATIVE DISULFIDE BONDED FOLDING INTERMEDIATES

Jiang, C., and  Chang, J.-Y. (2007)  Biochemistry   46, 602-609.
Isomers of Human a-Synuclein Stabilized by Disulfide Bonds Exhibit Distinct Structural and Aggregative Properties.

Zhang, Z., Boyle, P. C., Lu, B.-Y., Chang, J.-Y., and Wriggers, W. (2006)  Biochemistry   45, 15269-15278.
Entropic Folding Pathway of Human Epidermal Growth Factor Explored by Disulfide Scrambling and Amplified Collective Motion Simulation.

Lin  C.-J., Lu  B.-Y.,  and  Chang, J.-Y. (2006)  Biochem. Biophys. Acta   1764, 1286-1291.
Conformational Stability of Secretory Leucocyte Protease Inhibitor: A  PROTEIN WITH NO HYDROPHOBIC CORE AND VERY LITTLE SECONDARY STRUCTURE.
 
Salamanca, S.,  and  Chang, J.-Y.  (2006)  The Protein Journal  25, 275-287.
Pathway of Oxidative Folding of a 3-Disulfide a-Lactalbumin May Resemble Either BPTI Model or Hirudin Model.

Lin, C.-J. and  Chang, J.-Y. (2006)  Biochemistry  45, 6231-6240.
Pathway of Oxidative Folding of Secretory Leucocyte Protease Inhibitor: AN 8-DISULFIDES PROTEIN EXHIBITS A UNIQUE MECHANISM OF FOLDING

Arolas, J. L., Aviles, F. X.,  Chang, J.-Y. and Ventura, S. (2006) Trends In Biochem. Sci.  31, 292-301.
Folding of small disulfide-rich proteins: clarifying the puzzle.

Braun, M. C., Li, L., Ke, B., Dubinsky, W. P., Pickering, M. C. and  Chang, J.-Y. (2006)  Nephrology  26, 127-135.
Proteomic profiling of urinary protein excretion in the factor H-deficient mouse.

Chang, J.-Y.,   Lu, B.-Y., C. C.-J. Lin., and   C, Yu.  (2006)   FEBS Lett.  580, 656-660.
Fully Oxidized Scrambled Isomers Are Essential and Predominant Folding Intermediates of Cardiotoxin-III

Chang, J.-Y.,   Lu, B.-Y., and  Lai, P.-H.  (2006)   Biochem. J.   394, 249-257.
Oxidative folding of hirudin in human serum

Lu, B.-Y. Jiang, C., and  Chang, J.-Y. (2005)  Biochemistry 44, 15032-15041.
Isomers of Epidermal Growth Factor with Ser_Cys Mutation At the N-terminal Sequence: ISOMERIZATION, STABILITY, UNFOLDING, REFOLDING and STRUCTURE

Jiang, C., and  Chang, J.-Y. (2005)  FEBS Lett.  579, 3927-3931.
Unfolding and breakdown of insulin in the presence of endogenous thiol

Chang, J.-Y.,   Lu, B.-Y., and Li, L.  (2005)  Analytical  Biochemistry    342, 78-85.
Conformational impurity of disulfide proteins: Detection, quantification and properties 

Chang, J.-Y., and   Li, L. (2005)  Arch. Biochem. Biophys.  437, 85-95.
Divergent folding pathways of two homologous proteins, BPTI and tick anticoagulant peptide 

Lu, B.-Y.,  and  Chang, J.-Y.  (2005)  Analytical  Biochemistry  339, 94-103.
Assay of Disulfide Oxidase and Isomerase Based on  The Model of Hirudin Folding

Salamanca, S.,  and  Chang, J.-Y.  (2005)  Biochemistry  44,  744-750.
Unfolding and Refolding Pathways  of  A Major Kinetic Trap  in The Oxidative  Folding  of a-Lactalbumin

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