IR-spectroscopic characterization of an elongated OmpG mutant
Author:
Funder
Atilim University
TUBITAK
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics
Reference19 articles.
1. Biochemical and Biophysical Characterization of OmpG: A Monomeric Porin
2. Folding of a Monomeric Porin, OmpG, in Detergent Solution
3. pH-Induced Conformational Change of the β-Barrel-Forming Protein OmpG Reconstituted into Native E. coli Lipids
4. Structure of the monomeric outer-membrane porin OmpG in the open and closed conformation
5. pH-Dependent Interactions Guide the Folding and Gate the Transmembrane Pore of the β-Barrel Membrane Protein OmpG
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3. Investigations of pH-dependent dynamic properties of OmpG-16SL, an outer membrane protein G mutant by ATR-FTIR spectroscopy;Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics;2022-05
4. Inward-facing glycine residues create sharp turns in β-barrel membrane proteins;Biochimica et Biophysica Acta (BBA) - Biomembranes;2021-10
5. Manipulation of charge distribution in the arginine and glutamate clusters of the OmpG pore alters sugar specificity and ion selectivity;Biochimica et Biophysica Acta (BBA) - Biomembranes;2019-10
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