<i>In situ</i> opening/closing of OmpG from <i>E</i>. <i>coli</i> and the splitting of β-sheet signals in ATR-FTIR spectroscopy

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Date

2012

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Pergamon-elsevier Science Ltd

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Physics Group
Atılım University Physics Division was established with the purpose of educating the first-year students of the Engineering and other Departments by providing the general physics courses and, in addition, to make scientific and technological researches at the universal level. Now adays, Physics Division provide the students of Engineering, School of Aviation and Mathematics Departments with the general physics lectures having international education quality. We have in the Group the facilities of the mechanics and electricity laboratories, where the students have the opportunity to realize the practice of the theoretical knowledge in physics. Beside the compulsory courses (General Physics I and General Physics II) there are also elective courses offered by the Group. The faculty members in the Group, whose research interests and fields are given in web-page of the Group in details, perform theoretical as well as experimental researches and make publications in SSC-index journals. Graduate program, with master of sciences and doctorate degree courses and theses, is offered in different scientific areas (for details, see the web-page of the Division). In the Physcis Division there are 6 faculty members, five research assistants, and one technician.

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Abstract

The pH dependent opening and closure of Escherichia coli OmpG is driven by the formation and breaking of hydrogen bridges in beta-strands S11-S13. We have investigated the in situ secondary structural changes of OmpG with ATR-FTIR difference spectroscopy in order to detect the signals associated with the newly established interactions. Curve-fitting of OmpG in two pH conditions revealed the splitting and shifting of beta-sheet signals upon opening of the channel. Besides secondary structure changes, there are also amino acid side chain signals that play active role in opening/closing of the channel. An interaction among positively charged arginines and negatively charged aspartic and glutamic acid residues is suggested upon closure of the channel while this interaction is abolished when the channel opens at higher pH. (C) 2012 Elsevier B.V. All rights reserved.

Description

Korkmaz, Filiz/0000-0003-3512-3521; Yildiz, Ozkan/0000-0003-3659-2805

Keywords

beta-Barrel membrane protein, Secondary structure determination, FT-IR spectroscopy, Amide-I band analysis, Curve-fitting, Difference spectrum

Turkish CoHE Thesis Center URL

Citation

18

WoS Q

Q1

Scopus Q

Q1

Source

Volume

91

Issue

Start Page

395

End Page

401

URI

https://doi.org/10.1016/j.saa.2012.01.025
 https://hdl.handle.net/20.500.14411/1393

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