Investigations of pH-dependent dynamic properties of OmpG-16SL, an outer membrane protein G mutant by ATR-FTIR spectroscopy

Autor:	İrem Yılmaz, Filiz Korkmaz
Rok vydání:	2022
Předmět:	Escherichia coli Proteins Spectroscopy Fourier Transform Infrared Biophysics Porins Hydrogen-Ion Concentration Molecular Biology Biochemistry Protein Structure Secondary Analytical Chemistry Bacterial Outer Membrane Proteins
Zdroj:	Biochimica et biophysica acta. Proteins and proteomics. 1870(5)
ISSN:	1878-1454
Popis:	In this paper, the dynamic properties of outer membrane protein G mutant (OmpG-16SL) are investigated with ATR-FTIR spectroscopy. While OmpG-WT has 14 β-strands in its structure, the mutant is designed to have 16 β-strands with the intention of creating an enlarged pore. Loop L6 is elongated by introducing six residues, two of which are negatively charged. The solvent accessibility of the OmpG-16SL mutant is compared with WT and a previously reported mutant OmpG-16S by tracking the
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7bf0df62066aa01e51adb11c5c7c386b https://pubmed.ncbi.nlm.nih.gov/35405324 Zobrazit plný text záznamu Full Text from ScienceDirect