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Eric T. Baldwin
Researcher at Pfizer
Publications - 3
Citations - 166
Eric T. Baldwin is an academic researcher from Pfizer. The author has contributed to research in topics: Affinity chromatography & Ligand (biochemistry). The author has an hindex of 2, co-authored 3 publications receiving 155 citations.
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Journal ArticleDOI
Crystal Structure of the Herpes Simplex Virus 1 DNA Polymerase
Shenping Liu,John D. Knafels,Jeanne S. Chang,Gregory Allan Waszak,Eric T. Baldwin,Martin R. Deibel,Darrell R. Thomsen,Fred L. Homa,Peter A. Wells,Monica C. Tory,Roger A. Poorman,Hua Gao,Xiayang Qiu,Andrew P. Seddon +13 more
TL;DR: The first crystal structure of a herpesvirus polymerase is presented, the Herpes Simplex Virus type 1 DNA polymerase, at 2.7 Å resolution and a novel inhibition mechanism is proposed in which a representative of a series of non-nucleosidic viral polymerase inhibitors, the 4-oxo-dihydroquinolines, binds at the polymerase active site interacting non-covalently with both the polymer enzyme and the DNA duplex.
Journal ArticleDOI
Recombinant human cytomegalovirus protease with a C-terminal (His)6 extension: purification, autocatalytic release of the mature enzyme, and biochemical characterization.
Alfredo G. Tomasselli,D. J. Paddock,K. A. Curry,Robert L. Garlick,Joseph W. Leone,J. M. Lull,V. T. Mutchler,C. A. Baker,G. S. Cavey,W. R. Mathews,J.A. Shelly,B.C. Finzel,Eric T. Baldwin,P.A. Wells,C.-S. C. Tomich +14 more
TL;DR: To obtain large amounts of native protease, a 268-amino-acid polypeptide with a hexahistidinyl tag at the C terminus was expressed in Escherichia coli and refolded to an active enzyme using dialysis, similar to the enzymatic activity of CMV PR expressed as a soluble protein in E. coli.
Journal ArticleDOI
Affinity purification of a chimeric nicotinic acetylcholine receptor in the agonist and antagonist bound states
Shenping Liu,Merrill S. Babcock,Jacob Bode,Jeanne S. Chang,H. David Fischer,Robert L. Garlick,Gurnam S. Gill,Eric T. Lund,Brandon J. Margolis,W. Rodney Mathews,Bruce N. Rogers,Mark L. Wolfe,Vince Groppi,Eric T. Baldwin +13 more
TL;DR: A scalable path forward is suggested to generate multi-milligram amounts of purified complexes for additional studies including protein crystallization after the isolation of a mature alpha7/5HT(3) receptor with the signal peptide removed.