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Our research activities fall within 3 main areas, which all relate to the study of the kinetics and thermodynamics of protein conformational changes, namely membrane protein folding, protein-detergent interactions and protein fibrillation. These areas are linked by a keen interest in understanding the mechanistic and thermodynamic behaviour of proteins in different circumstances by quantifying the strength of internal side-chain interactions as well as contacts with solvent molecules, whether it be detergents, denaturants, stabilizing salts and osmolytes or lipids. Ultimately we hope this will lead to a greater manipulative ability vis-a-vis processes of both basic, pharmaceutical and industrial relevance. The general approach is to use available spectroscopic techniques (fluorescence, CD, stopped-flow, FTIR, NMR and dynamic and static light scattering) to generate data which can be analyzed in a quantitative manner to develop models and mechanisms for conformational changes at the molecular level.
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Journal of the American Chemical Societyno. 18 (2024): 12702-12711
International Dairy Journalpp.105946, (2024)
Nimrod Golan, Amit Parizat,Orly Tabachnikov,Eilon Barnea, William P. Olsen,Daniel E. Otzen,Meytal Landau
biorxiv(2024)
Farhang Aliakbari, Kimia Marzookian,Soha Parsafar,Hamdam Hourfar,Zahra Nayeri, Arghavan Fattahi, Mohammad Raeiji,Narges Nasrollahi Boroujeni,Daniel E Otzen,Dina Morshedi
Science advancesno. 14 (2024): eadl3406-eadl3406
ADVANCED MATERIALSno. 18 (2024): e2312823-e2312823
Free Radical Biology and Medicine (2024): 11-12
BBA Advances (2024): 100104-100104
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICSno. 2 (2024)
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