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[ Harvard iGEM]
[ Harvard iGEM]

Revision as of 15:09, 20 June 2007

Stephanie Lo
Harvard College 2010

c/o Harvard College PRISE
Leverett Mail Center
28 DeWolfe Street
Cambridge, MA 02138

I have always had a passion for sciences, particularly chemistry, and hope to pursue a joint concentration in Molecular and Cellular Biology and Economics. Eventually, I plan to apply for an MD/PhD program and specialize in digestive disorders.

NanoDrop results (6/20) performed by Ellenor and Stephanie:
(1.5 uL used out of a 30uL elution with nuclease free water)

S: 10.9 ng/uL
S2: 15.4 ng/uL
B: 59.1 ng/uL
B1: 25.1 ng/uL

Brainstorming for the two-component systems (really for my own use for now - not expected to be coherent)
Structural comparison of the PhoB and OmpR DNA binding/transactivation domains and the arrangement of PhoB molecules on the phosphate box
-NMR used to determine 3DE structure of PhoB DNA-binding/transactivation domain. Very similar to OmpR DNA-binding/transactivation domain, except for conformation of the long turn region of PhoB (interaction site for sigma subunit, rather than interaction with alpha subunit for OmpR)

Interdomain linkers of homologous response regulators determine their mechanism of action
Focuses on OmpR and PhoB and, as the title suggests, supports that phosphorylation of sites (particularly N-terminus of both proteins) improves affinity to bind DNA. Isolated C terminus of OmpR is insufficient to productively interact with RNA polymerase.
I've been told by some of the lab members that OmpR is an inner-membrane protein and therefore cannot be used for our assays. It seems that we'll have to find another protein ...

Harvard iGEM

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