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Daniel S. Kemp

 


Daniel S. Kemp Daniel S. Kemp
Professor of Chemistry
Room 18-584
(617) 253-1819
Fax: (617) 252-1609
kemp@mit.edu

B.A. Reed College 1958
Ph.D. Harvard University 1964


Research Summary
Proteins are linear polymers of roughly twenty natural amino acids, and the order in which particular amino acids appear along a given protein sequence determine its folding pattern and the overall shape of its folded or native conformation. This native conformation in turn controls the function of the protein in a living organism. A significant piece of the protein folding puzzle consists in determining how the sequence and amino acid composition of a medium-sized polypeptide governs the stability of helical conformations that can be formed from it.

Novel tools have recently been developed that allow this problem to be addressed incisively. (See: Kemp, D.S.; Allen,T.J.; Oslick, S.; Boyd, J.G. J. Am. Chem. Soc. (1995) 117 6641-6657. J. Am. Chem Soc. (1996) 118 4240-4248, 4249-4255.) This work depends on synthesis and study of novel bioorganic structures that are linked to normal polypeptides. These conjugates are characterized structurally by NMR and circular dichroism spectroscopy, as well as by other methods. Tailored Lifson-Roig matrix algorithms are used to analyze data and model helical stability. Projects within the scope of this problem involve a blend of bioorganic chemistry, synthetic organic chemistry, structural biology, and biophysics.

This research has two tightly coupled aims — first, development of a quantitatively accurate algorithm for predicting helicity from the amino acid sequence of peptide, and second, design, synthesis, and testing of "superhelical" analogs of the helix-stabilizing natural amino acids. These are expected to be uniquely incisive tools for studying a wide range of problems in medicinal chemistry, biophysics, and structural biology.

 

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