Stabilization of Therapeutic Proteins

Please use this identifier to cite or link to this item: http://dspace.mediu.edu.my:8181/xmlui/handle/1721.1/3794

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DC Field	Value	Language
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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