UM Biophysics Faculty

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Robert Zand

The Role of Molecular Structure in Determining Physical and Biological Properties of Proteins and Small Ligands

Zand

Professor-Biological Chemistry; Professor-Macromolecular Science & Engineering

Ph.D., Brandeis University

Dept: Biological Chemistry & Macromolecular Science & Engineering

Office Address: 4022 Chemistry

Phone: (734) 764-5138

Email: rzand@umich.edu

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.

Representative Publications

I.W.Kim, R. E. Robertson, andR. Zand (2005) Effects of Some Nonionic Polymeric Additives on the Crystallization of Calcium Carbonate, Crystal Growth and Design, 5, 513-522

V.A.Lee, R.G.Craig, F.E. Filisko and R. Zand, (2005) Microcalorimetry of the adsorption of lysozyme onto polymeric substrates, J.Colloid Interface Sci.288 6-13

K.Zhua, M.T. Kachman, F.R.Miller, D.M.Lubman, and R. Zand, (2004) Use of two dimensional liquid fractionation for separation of proteins from cell lysattes without the presence of meyhionine oxidation. Journal Chromatogr. A 1053, 133-142

C.D. Pointer-Keenan, D-K Lee, K. Hallok, A Tan, R.Zand and A. Ramamoorthy (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.

L. Klee, and Robert Zand (2004), Probable Epitopes: Relationships Between Myelin Basic Protein Antigenic Determinants and Viral and Bacterial Proteins Neuroinformatics 2, 59-70

J.K.Kim, R. Zand,.and D.M.Lubman, (2003), Electrophoretic mobility for peptides with post-translational modifications in capillary electophoresis, Electrophoresis 23, 782-793

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 .

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

Xiaoying Jin, Jeongkwon Kim, Stephen Parus, David M.Lubman*and Robert Zand, (1999) On-Line Capillary Electrophoresis/MicroElectrospray Ionization-Tandem Mass Spectrometry Using an Ion Trap Storage/Time of Flight Mass Spectrometer with SWIFT Technology, Anal. Chem 71, 3591-3597

Zand,R., Li, M.X., Jin, X., Lubman, D., (1998) Determination of the Sites of Posttranslational Modification in the Charge Isomers of Bovine Myelin Basic Protein by Capillary Electrophoresis-Mass Spectroscopy Biochemistry 37, 2441-2449

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Biophysics Research Division University of Michigan 4028 Chemistry Building 930 North University Avenue Ann Arbor, MI 48109-1055 UMsitemaker	Phone: (734) 763-6722 Fax: (734) 764-3323 E-mail: biophysics@umich.edu Last Updated: 5/25/2006 © Copyright 2006 University of Michigan