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Dr. Scholtz
http://mbch.tamu.edu/Pace_Scholtz/Default.htm We are currently applying a number of chemical and biophysical approaches to the study of protein folding and misfolding. Our major focus is to understand the forces that contribute to protein stability, to characterize the protein folding pathway and to study the mechanism(s) that give rise to protein misfolding and protein aggregation and amyloid formation. Our approaches are mainly experimental, but we are beginning to apply theory and computations to some of these problems. Our laboratory is very good at making careful measurements of the conformational changes of proteins and peptides and providing quantitative measurements of the kinetics and thermodynamics of folding and unfolding. We primarily employ a number of optical spectroscopic techniques to follow protein folding including circular dichroism, uv-absorbance and fluorescence. Several of the projects also employ NMR spectroscopy to probe structure, dynamics and local stability. We also use calorimetry, mass spectroscopy potentiometric titrations and electron microscopy for some of our studies. Our major focus over the next few years will be in protein aggregation and misfolding, and in electrostatic effects on protein stability and solubility. We are interested in the mechanism of amyloid formation in proteins and in devising or using small compounds to prevent protein aggregation and amyloid fibril formation. We will investigate how charge-charge interactions alter the biophysical properties of polypeptides and how they can be used to prevent aggregation. Each graduate student in my research group has his or her own project investigating a specific set of questions and each is responsible for carrying out all aspects of the project. Each student therefore learns and does all of the techniques required to complete the project. Typically this would involve routine molecular biology techniques to construct synthetic genes, protein expression and purification and finally, analysis using a battery of spectroscopic techniques. In many cases these projects also involve the synthesis and characterization of small peptides. Increasingly we are using computational methods to help us design experiments or interpret the results. |
