Replacing the eleven native P-glycoprotein tryptophans by directed evolution produces an active protein with site-specific, non-conservative substitutions.

Douglas J Swartz; Anukriti Singh; Narong Sok; Joshua N Thomas; Joachim Weber; Ina L Urbatsch

Replacing the eleven native P-glycoprotein tryptophans by directed evolution produces an active protein with site-specific, non-conservative substitutions.

Douglas J Swartz, Anukriti Singh, Narong Sok, Joshua N Thomas, Joachim Weber, Ina L Urbatsch

Chemistry and Biochemistry

Research output: Contribution to journal › Article › peer-review

Original language	English
Pages (from-to)	3224
Journal	Scientific reports
State	Published - Jan 2020

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@article{94018ac1498f4509b1896d9e4ca69c0a,

title = "Replacing the eleven native P-glycoprotein tryptophans by directed evolution produces an active protein with site-specific, non-conservative substitutions.",

author = "Swartz, {Douglas J} and Anukriti Singh and Narong Sok and Thomas, {Joshua N} and Joachim Weber and Urbatsch, {Ina L}",

year = "2020",

month = jan,

language = "English",

pages = "3224",

journal = "Scientific reports",

publisher = "Nature Springer",

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TY - JOUR

T1 - Replacing the eleven native P-glycoprotein tryptophans by directed evolution produces an active protein with site-specific, non-conservative substitutions.

AU - Swartz, Douglas J

AU - Singh, Anukriti

AU - Sok, Narong

AU - Thomas, Joshua N

AU - Weber, Joachim

AU - Urbatsch, Ina L

PY - 2020/1

Y1 - 2020/1

M3 - Article

SP - 3224

JO - Scientific reports

JF - Scientific reports

ER -

Replacing the eleven native P-glycoprotein tryptophans by directed evolution produces an active protein with site-specific, non-conservative substitutions.

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