Jean Baum
Professor

NMR. protein folding. molecular recognition

Our research involves the development and application of nuclear magnetic resonance (NMR) spectroscopy to the study of proteins. Methods of high-resolution NMR in conjunction with computer algorithms are used to examine the dynamics and three-dimensional structures of proteins in solution.

One area of interest is to use NMR to understand the manner in which a protein folds from an unstructured state to its final compact globular structure. The study of the folding intermediates may provide a description of the pathways by which this important process occurs. A second area of interest involves protein-protein interactions and molecular recognition in proteins of medical and biological interest. The emphasis of the research is to develop novel NMR methods and apply existing techniques to model peptide and protein systems in order to explore these important problems in biophysical chemistry.

Selected Publications

Weinstock DS, Narayanan C, Baum J, Levy RM. (2008) Correlation between 13Calpha chemical shifts and helix content of peptide ensembles. Protein Sci. 17(5):950-4.

Go A, Kim S, Baum J, Hecht MH. (2008) Structure and dynamics of de novo proteins from a designed superfamily of 4-helix bundles. Protein Sci. 17(5):821-32.

Wu KP, Kim S, Fela DA, Baum J. (2008) Characterization of conformational and dynamic properties of natively unfolded human and mouse alpha-synuclein ensembles by NMR: implication for aggregation. J Mol Biol. 378(5):1104-15.

Thiagarajan G, Li Y, Mohs A, Strafaci C, Popiel M, Baum J, Brodsky B. (2008) Common interruptions in the repeating tripeptide sequence of non-fibrillar collagens: sequence analysis and structural studies on triple-helix peptide models. J Mol Biol. 376(3):736-48.

Andersen D, Storz T, Liu P, Wang X, Li L, Fan P, Chen X, Allgeier A, Burgos A, Tedrow J, Baum J, Chen Y, Crockett R, Huang L, Syed R, Larsen RD, Martinelli M. (2007) Stereoselective synthesis of a MCHr1 antagonist. J Org Chem. 72(25):9648-55.

Li Y, Brodsky B, Baum J. (2007) NMR shows hydrophobic interactions replace glycine packing in the triple helix at a natural break in the (Gly-X-Y)n repeat. J Biol Chem. 282(31):22699-706.

Weinstock DS, Narayanan C, Felts AK, Andrec M, Levy RM, Wu KP, Baum J. (2007) Distinguishing among structural ensembles of the GB1 Peptide: REMD simulations and NMR experiments. J Am Chem Soc. 129(16):4858-9.

Hyde TJ, Bryan MA, Brodsky B, Baum J. (2006) Sequence dependence of renucleation after a Gly mutation in model collagen peptides. J Biol Chem. 281(48):36937-43.

Mohs A, Popiel M, Li Y, Baum J, Brodsky B. (2006) Conformational features of a natural break in the type IV collagen Gly-X-Y repeat. J Biol Chem. 281(25):17197-202.

Wang X. Zhi B. Baum J. Chen Y. Crockett R. Huang L. Eisenberg S. Ng J. Larsen R. Martinelli M. Reider P. (2006) A Practical Synthesis of 2-((1H-Pyrrolo[2,3-b]pyridine-4-yl)methylamino)-5- fluoronicotinic Acid. J Org Chem. 71(10):4021-3.

Mohs. A.. Li. Y.. Doss-Pepe. E.. Baum. J. and Brodsky. B.(2005) Stability junction at a common mutation site in the collagenous domain of the mannose binding lectin. Biochemistry 44: 1793.

Buevich. A.. Silva. T.. Brodsky. B. and Baum. J. (2004) Transformation of the mechanism of triple-helix peptide folding in the absence of a C-terminal nucleation domain and its implications for mutations in collagen disorders. J. Biol. Chem. 279:46890.

Kim. S. and Baum. J. (2004) An on/off resonance rotating frame experiment to monitor millisecond to microsecond timescale dynamics. Journal of Biomolecular NMR 30:195.

Xu. Y.. Hyde. T.. Wang. X.. Bhate. M.. Brodsky. B. and Baum. J. (2003) NMR and CD evidence for efficient folding of a triple-helical peptide by imino acid restriction of the unfolded state. Biochemistry 42:8696.

Wei. Y.. Kim. S.. Fela. D.. Baum. J.. Hecht. M. (2003) Solution structure of a de novo protein from a designed combinatorial library. Proceedings of the National Academy of Science 100:13270.

Buevich. A. and Baum. J.(2002) Defining the aggregation states of protein folding intermediates by residue specific real time NMR diffusion experiments. J. Am. Chem. Soc. 124:7156.