Structural proteomics : elucidating in vivo structural dynamics of integral membrane proteins by hydroxyl radical footprinting

We have developed a in vivo hydroxyl radical protein footprinting method for investigating the structure-function relationship of three distinct yet common classes of membrane proteins, a porin protein (OmpF) involved in voltage gating, a heterodimer (integrin αLβ2) important in cell adhesion and si...

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Bibliographic Details
Main Author: Zhu, Yi
Other Authors: Sze Siu Kwan
Format: Thesis
Language:English
Published: 2012
Subjects:
Online Access:https://hdl.handle.net/10356/48373
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author Zhu, Yi
author2 Sze Siu Kwan
author_facet Sze Siu Kwan
Zhu, Yi
author_sort Zhu, Yi
collection NTU
description We have developed a in vivo hydroxyl radical protein footprinting method for investigating the structure-function relationship of three distinct yet common classes of membrane proteins, a porin protein (OmpF) involved in voltage gating, a heterodimer (integrin αLβ2) important in cell adhesion and signaling, and a receptor-ligand interaction (EGF-EGFR) of a typical receptor tyrosine kinase essential for cell growth and signaling. This work indicates that the hydroxyl radical footprinting technique is a promising approach to study the structural dynamics of the integral membrane proteins directly in the native environment on the cell surfaces, and furthermore, to understand the biological function of this important class of proteins that is challenging to be studied by other structural biological methods.
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spelling ntu-10356/483732023-02-28T18:33:55Z Structural proteomics : elucidating in vivo structural dynamics of integral membrane proteins by hydroxyl radical footprinting Zhu, Yi Sze Siu Kwan School of Biological Sciences DRNTU::Science::Biological sciences We have developed a in vivo hydroxyl radical protein footprinting method for investigating the structure-function relationship of three distinct yet common classes of membrane proteins, a porin protein (OmpF) involved in voltage gating, a heterodimer (integrin αLβ2) important in cell adhesion and signaling, and a receptor-ligand interaction (EGF-EGFR) of a typical receptor tyrosine kinase essential for cell growth and signaling. This work indicates that the hydroxyl radical footprinting technique is a promising approach to study the structural dynamics of the integral membrane proteins directly in the native environment on the cell surfaces, and furthermore, to understand the biological function of this important class of proteins that is challenging to be studied by other structural biological methods. DOCTOR OF PHILOSOPHY (SBS) 2012-04-09T01:39:48Z 2012-04-09T01:39:48Z 2012 2012 Thesis Zhu, Y. (2012). Structural proteomics : elucidating in vivo structural dynamics of integral membrane proteins by hydroxyl radical footprinting. Doctoral thesis, Nanyang Technological University, Singapore. https://hdl.handle.net/10356/48373 10.32657/10356/48373 en 155 p. application/pdf
spellingShingle DRNTU::Science::Biological sciences
Zhu, Yi
Structural proteomics : elucidating in vivo structural dynamics of integral membrane proteins by hydroxyl radical footprinting
title Structural proteomics : elucidating in vivo structural dynamics of integral membrane proteins by hydroxyl radical footprinting
title_full Structural proteomics : elucidating in vivo structural dynamics of integral membrane proteins by hydroxyl radical footprinting
title_fullStr Structural proteomics : elucidating in vivo structural dynamics of integral membrane proteins by hydroxyl radical footprinting
title_full_unstemmed Structural proteomics : elucidating in vivo structural dynamics of integral membrane proteins by hydroxyl radical footprinting
title_short Structural proteomics : elucidating in vivo structural dynamics of integral membrane proteins by hydroxyl radical footprinting
title_sort structural proteomics elucidating in vivo structural dynamics of integral membrane proteins by hydroxyl radical footprinting
topic DRNTU::Science::Biological sciences
url https://hdl.handle.net/10356/48373
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