Date of Award

1-1-2015

Language

English

Document Type

Dissertation

Degree Name

Doctor of Philosophy (PhD)

College/School/Department

Department of Chemistry

Content Description

1 online resource (x, 104 pages) : color illustrations.

Dissertation/Thesis Chair

Alexander Shekhtman

Committee Members

Marlene Belfort, Igor Lednev, Li Niu, Maksim Royzen

Keywords

In-Cell, Nuclear Magnetic Resonance, Proteins, Quinary Structure, RNA, Structural Biology, Nuclear magnetic resonance spectroscopy, Protein folding

Subject Categories

Biochemistry | Chemistry

Abstract

Nuclear Magnetic Resonance Spectroscopy (NMR) is one of the principle tools in structural biology to probe macromolecular structures and interactions. The atomic resolution afforded by this technique has been widely used to probe protein-protein, and protein-ligand interactions in-vitro. However, the natural milieu of the proteins is the living cell and the cellular cytoplasm is extremely heterogeneous. The NMR studies of folded protein in-cell, till now, have been limited by non-specific interactions of the cytosol. This thesis outlays a general methodology to study protein structure/interactions inside the living cells using NMR. In a closely related objective, it also describes the use of advanced statistical methods to interpret the binding of an unstructured protein to its cognate partner, inside the cytosol. Finally, it demonstrates the ability of NMR to calculate structure of protein-complexes having functional consequences. Overall, this thesis aims to bridge the gap between in-vitro structure and in-cell functional studies.

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