Date of Award

1-1-2017

Language

English

Document Type

Dissertation

Degree Name

Doctor of Philosophy (PhD)

College/School/Department

Department of Chemistry

Content Description

1 online resource (ii, xiii, pages) : illustrations (some color)

Dissertation/Thesis Chair

Alexander Shekhtman

Committee Members

Jia Sheng, Jayanti Pande, Kathleen A. McDonough

Keywords

In-cell NMR, Quinary interactions, Nuclear magnetic resonance spectroscopy, Proteins, Mycobacterium bovis

Subject Categories

Biochemistry | Chemistry

Abstract

Intrinsically disordered proteins or unstructured segments within proteins play an important role in cellular physiology and pathology. A combination of peptide aptamers selected by using the yeast-two-hybrid scheme, and in-cell NMR identified high affinity binders to a transiently structured intrinsically disordered proteins (IDP). This method was validated using the prokaryotic ubiquitin-like protein, Pup, of the Mycobacterium proteasome. We discover two peptide aptamers that bind to opposite sites of a transient helix in Pup, an intrinsically disordered protein, that have vastly different effects on the survival of Mycobacterium bovis BCG.

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