Show simple item record

dc.contributor.advisorStewart, Mikaela
dc.contributor.authorLee, Jane
dc.date5/19/2021
dc.date.accessioned2021-10-25T21:48:46Z
dc.date.available2021-10-25T21:48:46Z
dc.date.issued2021
dc.identifier.urihttps://repository.tcu.edu/handle/116099117/49055
dc.description.abstractMutations in BReast CAncer 1 protein (BRCA1) play a crucial role in DNA damage control such as double-strand DNA break repair mechanisms. Mutations in BRCA1 increase the chance of disrupted genetic integrity by their contributions to the development of breast cancer. BRCA1 must bind to its partner protein, Partner and Localizer to BRCA2 (PALB2), in order to properly carry out its function in the repair mechanism pathway, but its conformation once bound to PALB2 is not clear. In its active state, PALB2 is known to remain in an alpha-helical coiled-coil homodimer conformation. Through this observation, we hypothesized that the intrinsically disordered region of BRCA1 on its binding surface will undergo a conformational change into an alpha-helical form. In order to test this hypothesis, we first created a truncated BRCA1, making it 50 amino acids long, then conducted nuclear magnetic resonance experiments (NMR). Through the NMR experiments, we found that the binding interface of BRCA1 does change its conformation into a helical state, forming a coiled-coil heterodimer upon binding with PALB2.
dc.titleInvestigating The Effects Of Brca1 Construct Length On Its Interaction With Palb2
etd.degree.departmentBiology
local.collegeCollege of Science and Engineering
local.collegeJohn V. Roach Honors College
local.departmentBiology


Files in this item

Thumbnail
This item appears in the following Collection(s)

Show simple item record