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Stabilization of Therapeutic Proteins

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dc.creator Chu, Jhih-Wei
dc.creator Yin, Jin
dc.creator Mazyar, Oleg
dc.creator Goh, Lin-Tang
dc.creator Yap, Miranda G.S.
dc.creator Wang, Daniel I.C.
dc.creator Trout, Bernhardt L.
dc.date 2003-12-08T16:17:14Z
dc.date 2003-12-08T16:17:14Z
dc.date 2003-01
dc.date.accessioned 2013-10-09T02:32:30Z
dc.date.available 2013-10-09T02:32:30Z
dc.date.issued 2013-10-09
dc.identifier http://hdl.handle.net/1721.1/3794
dc.identifier.uri http://koha.mediu.edu.my:8181/xmlui/handle/1721
dc.description We present results of molecular simulations, quantum mechanical calculations, and experimental data aimed towards the rational design of solvent formulations. In particular, we have found that the rate limitation of oxidation of methionine groups is determined by the breaking of O-O bonds in hydrogen peroxide, not by the rate of acidic catalysis as previously thought. We have used this understanding to design molecular level parameters which are correlated to experimental data. Rate data has been determined both for G-CSF and for hPTH(1-34).
dc.description Singapore-MIT Alliance (SMA)
dc.format 1694999 bytes
dc.format application/pdf
dc.language en_US
dc.relation Molecular Engineering of Biological and Chemical Systems (MEBCS);
dc.subject protein stabilization
dc.subject excipients
dc.subject molecular simulations
dc.subject kinetics
dc.title Stabilization of Therapeutic Proteins
dc.type Article


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