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Our research is primarily focused on the use of spectroscopic techniques to determine biomolecular structure and follow its dynamic changes. My group is recognized for developing new IR and vibrational circular dichroism (VCD) based optical spectroscopic methods and applying them to the study of peptide and protein conformation and folding. We have developed ab initio QM methods to model and interpret our peptide IR, Raman and VCD spectra. Our spectral studies probe equilibrium and thermodynamic changes, as well as microsec dynamics using IR and fluorescence detected T-jump methods. Most of these studies address model peptide systems to exemplify fundamental secondary structure types and to model small folding units in proteins. Our studies also use NMR structure determination to generate models for folded structures and MD methods to develop models for folding processes and intermediate structures on the pathway. Recently we have begun studies related to protein and peptide aggregation and fibril formation, processes important in many biomedical conditions.
Additionally, the group previously studied folding of larger proteins, with an emphasis on b-sheet dominant structures, aggregates, and models for protein membrane interaction and folding studies. Perturbation effects on protein and protein complex structures, such as disulfide reduction, surface binding, pH and thermal variation are studied with equilibrium and dynamic (stop-flow) IR, CD and fluorescence methods.
Earlier work allowed us to refine protein structure determination in terms of fractional secondary structure with using various pattern recognition and statistical methods to interpret optical spectra, which can correlate with NMR studies, H-D exchange, as well as kinetically based fluorescence and electronic CD spectral measurements. All of these are useful for dynamic study of structural changes such as occur during the protein folding process.
Additionally, the group previously studied folding of larger proteins, with an emphasis on b-sheet dominant structures, aggregates, and models for protein membrane interaction and folding studies. Perturbation effects on protein and protein complex structures, such as disulfide reduction, surface binding, pH and thermal variation are studied with equilibrium and dynamic (stop-flow) IR, CD and fluorescence methods.
Earlier work allowed us to refine protein structure determination in terms of fractional secondary structure with using various pattern recognition and statistical methods to interpret optical spectra, which can correlate with NMR studies, H-D exchange, as well as kinetically based fluorescence and electronic CD spectral measurements. All of these are useful for dynamic study of structural changes such as occur during the protein folding process.
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SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY (2024): 124097-124097
CHEMICAL REVIEWSno. 7 (2020): 3381-3419
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