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Full-Text Articles in Physical Sciences and Mathematics
Chemistry Of Hydrogen Oxide Radicals (Hox) In The Arctic Troposphere In Spring, J Mao, D J. Jacob, M J. Evans, J R. Olson, X Ren, W H. Brune, T M. St. Clair, J D. Crounse, K M. Spencer, M R. Beaver, P O. Wennberg, M J. Cubison, J L. Jimenez, A Fried, P Weibring, J G. Walega, S R. Hall, A J. Weinheimer, R C. Cohen, G Chen, J H. Crawford, C Mcnaughton, A D. Clarke, L Jaegle, Jenny A. Fisher, R M. Yantosca, P Le Sager, C C. Carouge
Chemistry Of Hydrogen Oxide Radicals (Hox) In The Arctic Troposphere In Spring, J Mao, D J. Jacob, M J. Evans, J R. Olson, X Ren, W H. Brune, T M. St. Clair, J D. Crounse, K M. Spencer, M R. Beaver, P O. Wennberg, M J. Cubison, J L. Jimenez, A Fried, P Weibring, J G. Walega, S R. Hall, A J. Weinheimer, R C. Cohen, G Chen, J H. Crawford, C Mcnaughton, A D. Clarke, L Jaegle, Jenny A. Fisher, R M. Yantosca, P Le Sager, C C. Carouge
Faculty of Science - Papers (Archive)
We use observations from the April 2008 NASA ARCTAS aircraft campaign to the North American Arctic, interpreted with a global 3-D chemical transport model (GEOS-Chem), to better understand the sources and cycling of hydrogen oxide radicals (HOx≡H+OH+peroxy radicals) and their reservoirs (HOy≡HOx+peroxides) in the springtime Arctic atmosphere. We find that a standard gas-phase chemical mechanism overestimates the observed HO2 and H2O2 concentrations. Computation of HOx and HOy gas-phase chemical budgets on the basis of the aircraft observations also indicates a large missing sink for both. We hypothesize that …
Protein Chemistry Of Amyloid Fibrils And Chaperones: Implications For Amyloid Formation And Disease, Justin J. Yerbury, Janet R. Kumita
Protein Chemistry Of Amyloid Fibrils And Chaperones: Implications For Amyloid Formation And Disease, Justin J. Yerbury, Janet R. Kumita
Faculty of Science - Papers (Archive)
Understanding the mechanisms by which amyloid fibrils are formed, both in vivo and in vitro, is vital for developing methods to treat and prevent debilitating deposition diseases such as Alzheimer's disease, Parkinson's disease, type II diabetes and systemic amyloidoses. In recent years, computer modelling and biophysical studies have broadened our understanding of the biochemical mechanisms underpinning protein aggregation. As a result, it is now believed that the ability to form fibrils is an intrinsic property of polypeptide chains and not isolated to disease-related proteins or peptides. Molecular chaperones are a diverse group of functionally related proteins well known for their …