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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Format: | Thesis |
Language: | English |
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2012
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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. |
first_indexed | 2024-10-01T03:18:04Z |
format | Thesis |
id | ntu-10356/48373 |
institution | Nanyang Technological University |
language | English |
last_indexed | 2024-10-01T03:18:04Z |
publishDate | 2012 |
record_format | dspace |
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 |
work_keys_str_mv | AT zhuyi structuralproteomicselucidatinginvivostructuraldynamicsofintegralmembraneproteinsbyhydroxylradicalfootprinting |