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Ari Gafni |
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Professor Biological Chemistry Research Professor |
 Ari Gafni |
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Biophysics Research Division |
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Ph.D., Weizmann Institute |
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| Office Address: 3204 Chemistry | ||||||||
| Phone: (734) 615-1964 | ||||||||
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Email: arigafni@umich.edu |
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| Current
research in our laboratory focuses on mechanistic aspects of protein
folding, on the identification of molecular interactions that stabilize
the folded state, and on the characterization of those alterations in
the folded structure that occur during aging and in some age-associated
diseases. Of particular interest in the latter category are the
structural alterations that lead to the aggregation of protein
molecules into amyloid deposits, the hallmark of several devastating
human diseases including Alzheimer’s disease and non-insulin-dependent
diabetes. While the concept that the three dimensional structure of a
protein is encoded in its amino acid sequence is a central tenet of
contemporary biology, it is still unclear how this information is
utilized in directing the polypeptide chain to fold into a unique,
biologically active, structure. This problem, often termed "the second
half of the genetic code," is of great importance because its solution
will allow us to predict structures of proteins from their amino acids
sequences (from genetic information), and to engineer more stable,
longer lived, proteins by introducing appropriate mutations. This
understanding will also open the door for engineering proteins with new
structures and functions. Our elucidation of the structural evolution of the folded state of proteins is accomplished by a variety of molecular-biological, biochemical and biophysical approaches. Laser-based optical spectroscopic techniques, and in particular time-resolved room-temperature phosphorescence, fluorescence, and light scattering are used to follow protein folding, misfolding and aggregation in real time and serve in the development and testing of strategies for the inhibition of amyloid production. Of special importance to these studies is our application of single molecule spectroscopy, a technique that provides unprecedented resolving power since it is free from ensemble averaging, to address mechanistic details of protein interactions and structural transitions that can not be resolved by conventional experimental approaches. |
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Representative Publications |
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Wisser KC, Schauerte JA, Burke DT, Galecki AJ, Chen S, Miller RA and Gafni A: Mapping tissue-specific genes correlated with age-dependent changes in protein stability and function. Arch. Biochem. Biophys. 2004; 432: 58-70. |
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