Analysis of the Secondary Structure of the Transmembrane Domain of SARS CoV E Protein using FTIR Spectroscopy
Date
2007-05-10
Authors
قاسم موسى هاشم أبو رميله
Qassem Mussa Hashem Abu Rmeleh
Journal Title
Journal ISSN
Volume Title
Publisher
AL-Quds University
جامعة القدس
جامعة القدس
Abstract
One of the major obstacles facing the field of structural biology in the postgenomic era is
the inherent difficulty of solving the structure of membrane proteins under native
conditions. Membrane proteins share a common property; part of their structure is
embedded in the lipid bilayer. This feature makes them attractive drug targets, which
requires a detailed knowledge of the secondary structure of their transmembrane domain.
Both crystallography and NMR still encounter difficulties in handling membrane proteins,
so there is an urgent need for new biophysical methods and new insights in the biophysics
of membrane proteins to solve the secondary structure of such proteins.
The outbreak of the severe acute respiratory syndrome (SARS) virus, July 2003, has
presented a formidable challenge for the scientific community. As part of that effort, we
decided to study the high resolution backbone structure of E transmembrane proteins of the
SARS coronavirus, by Attenuated Total Internal Reflection (ATR) FTIR of eighteen of
isotopically labeled sites with (
13C=18O) of the synthesized sequence for the SARS
coronavirus E protein transmembrane domain. ATR-FTIR spectroscopy is a wellestablished
method for generating precise structural information on isotopically labeled
membrane proteins embedded in a lipid bilayer. We used the new biophysical method site
specific infrared dichroism (SSID), to investigate the structure and orientation of
transmembrane. α-helical bundles
We postulate in this work that the E protein of SARS CoV is α-helix, and it has 26 residues
embedded in the lipid bilayer, and the SARS CoV E protein is not a regular helix, but it
adopts a unique transmembrane helical hairpin model, and the E protein has two possible
kinks at residue No. 26 and 31 Phe and Leu respectively within the lipid bilayer, which isreported for the first time in this thesis. And it also has a possible kink in residue No 15 too.
All the results were confirmed experimentally.
Description
Keywords
الكيمياء الحيوية والاحياء الجزيئية , Biochemistry & Molecular Biology