TY - GEN AB - The goal of this research is to characterize the contribution of histidine and methionine to function in copper proteins. The emergence of His and Met residues in copper proteins is not new, but the flexible dynamic provided is novel and has been shown to alter function. We have characterized the pH-­‐dependent coordination chemistry involving His-­‐Met residues in cuproproteins peptidylglycine hydroxylating monooxygenase (PHM) and the HM Loop of ATP7A, which is involved in copper translocation. AD - Oregon Health and Science University AU - Kline, Chelsey DA - 2015 DO - 10.6083/M4XW4HJ2 DO - DOI ED - Blackburn, Ninian ED - Mayfield, Mary ED - Advisor ED - Mentor ID - 2880 KW - Copper KW - Biological Transport KW - X-Ray Absorption Spectroscopy KW - Biochemistry L1 - https://digitalcollections.ohsu.edu/record/2880/files/3649_etd.pdf L2 - https://digitalcollections.ohsu.edu/record/2880/files/3649_etd.pdf L4 - https://digitalcollections.ohsu.edu/record/2880/files/3649_etd.pdf LK - https://digitalcollections.ohsu.edu/record/2880/files/3649_etd.pdf N2 - The goal of this research is to characterize the contribution of histidine and methionine to function in copper proteins. The emergence of His and Met residues in copper proteins is not new, but the flexible dynamic provided is novel and has been shown to alter function. We have characterized the pH-­‐dependent coordination chemistry involving His-­‐Met residues in cuproproteins peptidylglycine hydroxylating monooxygenase (PHM) and the HM Loop of ATP7A, which is involved in copper translocation. PB - Oregon Health and Science University PY - 2015 T1 - Histidine-methionine contributions to function in copper proteins TI - Histidine-methionine contributions to function in copper proteins UR - https://digitalcollections.ohsu.edu/record/2880/files/3649_etd.pdf Y1 - 2015 ER -