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		Daniel P. Raleigh Professor B.A., Chemistry and Mathematics, 1981, Humboldt State University; Ph.D. 1988, Massachusetts Institute of Technology; Helen Hay Whitney Fellowship, University of Oxford, 1988-1991; Postdoctoral Fellow, The DuPont Merck Co., 1991-1993; Pew Scholar in the Biomedical Sciences 1995-Present; National Science Foundation Career Award 1996-2000. (631) 632-9547 Email: draleigh@notes.cc.sunysb.edu Publications

	STRUCTURAL BIOLOGY The research in our group is centered upon studies of protein folding, protein structure and the mechanism of amyloid formation. We want to understand how proteins fold to their final three dimensional structure and we want to understand why the folded conformation of proteins is stable. Our work on amyloid formation is directed towards understanding the physical basis for the pathological aggregation of polypeptides in certain diseases. These projects involve a wide range of techniques, including but not limited to: high resolution multidimensional NMR, protein design, stop flow methods, peptide synthesis and protein chemistry. Protein Folding Elucidating how the amino acid sequence determines structure, the protein folding problem, is a central issue in modern structural biology. Our laboratory is currently studying the folding of two proteins, the ribosomal protein L9 and the E3/E1p-binding domain. A second area of interest is the nature of partially folded states of proteins. In recent years it has become clear that many proteins can exist in a partially folded state, known as the molten globule state, which contains a high degree of secondary structure but which lacks fixed tertiary interactions. We are studying the molten globule state formed by a small calcium binding protein, a-lactalbumin. Our studies of natural proteins are complemented by efforts in de novo protein design. Amyloid Formation In certain diseases normally soluble proteins aggregate to form a dense structure called the amyloid fibril. Amyloid deposits are present in individuals suffering from type-II diabetes, Alzheimer's disease and in patients undergoing kidney dialysis. Little is known about the molecular mechanism of amyloid formation. We are studying amyloid formation by the polypeptides amylin and calcitonin. Amylinis a 37 residue peptide which forms amyloid deposits in type-II diabetes while calcitonin forms amyloid deposits in the thyroid. Our work involves the preparation of the peptides via solid phase peptide synthesis, the characterization of the structure of these molecules and studies of the kinetics of amyloid formation.

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