Professor, Biological Chemistry
B.S., University of Missouri
M.S., Polytechnic Institute of New York
Ph.D., Brandeis University
Postdoctoral, Harvard Medical School
The research in my laboratory is directed at understanding the role of posttranslational modifications on a central nervous system protein present in the myelin membrane. This protein known as the myelin basic protein (MBP) is known to be extensively posttranslationally modified by phosphorylation, methylation, and deimination. In addition, the protein binds Zinc, copper and other metal ions. Many of these modifications are known to be involved in a number of human pathologies of which the most well known one is multiple sclerosis. My laboratory studies the presence of these posttranslational modifications in MBP, identifies the amino acids that are modified, and if that modification is involved in the aberent behavior of the membrane. One extreme example of this occurs in a severe form of Multiple Sclerosis in which the amino acid arginine present in MBP is converted into the amino acid citrulline. In MBP there are 19 arginine residues and in the form of MS known as Marburgs disease, 18 of the 19 arginine residues are converted into citrulline. This removes 18 positive charges from the protein and must result in a change in coformation and in its ability to function normally thereby permitting attacking on the membrane by the immune system. We study the changes in the MBP using mass spectrrometry, Circular Dichroism, NMR, FTIR and other spectroscopic techniques.
Another area of MBP interest is how it has changed in primary structure through evolution. Once the sequence of MBP from a particular species has been identified It can be analyzed relative to its position in the evolutionary chain. This also allows for an assessment of the posttranslational modifications and the primary structure.
2004-2007 Jordi Folch-Pi Award Committee-American Society for Neurochemistry
I.W.Kim, R. E. Robertson, and R. Zand (2005) Effects of Some Nonionic Polymeric Additives on the Crystallization of Calcium Carbonate, Crystal Growth and Design, In Press http://pubs.acs.org/doi/abs/10.1021/cg049721q
C.D. Pointer-Keenan, D-K Lee, K. Hallok, A Tan, R.Zand and A. Ramamoorth (2004) Investigation of the interaction of myelin basic protein with phospholipid bilayers using solid state NMR spectroscopy, Chem. and Physics of Lipids,132, 47-54.
K.Zhua, M.T. Kachman, F.R.Miller, D.M.Lubman, and R. Zand, (2004) Use of two dimensional liquid fractionation for deparation of proteins from cell lysattes without the presence of meyhionine oxidation. Journal Chromatogr. A 1053, 133-142
L. Klee, and Robert Zand (2004), Probable Epitopes: Relationships Between Myelin Basic Protein Antigenic Determinants and Viral and Bacterial Proteins. Neuroinformatics 2, 59-70PMID: 15067168
J.K. Kim, F. G. Mastronardi, D.D. Wood, D.M. Lubman, M. A. Moscarello and R. Zand (2003), Multiple Sclerosis: An Important Role for Post-Translational Modifications in Pathogenesis, Molecular and Cell. Proteomics 2, 443-452 PMID: 12832457
I-W Kim, R,E, Robertson and R. Zand, (2003) Selected Polymorphs of CaCO3 Through Epitaxy with Inorganic Substrates Aligned with an Electric Field, Adv. Mater. 15, 709-712
J.K.Kim, R. Zand,.and D.M.Lubman, (2003), Electrophoretic mobility for peptides with post-translational modifications in capillary electophoresis, Electrophoresis 23, 782-793PMID: 12627438
R. Zand,, X. Jin, J.Kim, D.B. Wall, R. Gould, and D.M.Lubman, (2001) Studies of Posttranslational Modification in Spiny Dogfish Myelin Basic Protein Neurochem. Res. 26, 539-547
R. Zand, (2001) Ethical Responsibilities of the Principal Investigator, in New Ethical Challenges in Science and Technology, Sigma Xi Forum Nov 9-10, 2000 pp79-83