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Günnur Güler

Researcher at İzmir University of Economics

Publications -  18
Citations -  365

Günnur Güler is an academic researcher from İzmir University of Economics. The author has contributed to research in topics: Fourier transform infrared spectroscopy & Protein secondary structure. The author has an hindex of 8, co-authored 16 publications receiving 263 citations. Previous affiliations of Günnur Güler include İzmir Institute of Technology & Ege University.

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Proteolytically-induced changes of secondary structural protein conformation of bovine serum albumin monitored by Fourier transform infrared (FT-IR) and UV-circular dichroism spectroscopy

TL;DR: Both spectroscopic techniques demonstrate that there are similar but less spectral changes of BSA for the trypsin attack than for α-chymotrypsin although the substrate/enzyme ratio is taken the same.
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A novel method for sensitive microRNA detection: Electropolymerization based doping.

TL;DR: For the first time, sensitive electrochemical detection of a breast cancer biomarker microRNA (miRNA), mir-21 was achieved via electropolymerized polypyrrole ( PPy) modified pencil graphite electrodes (PPy/PGE), through hybridization of electrochemically doped probe miRNA, antimir-21.
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Real time observation of proteolysis with Fourier transform infrared (FT-IR) and UV-circular dichroism spectroscopy: watching a protease eat a protein.

TL;DR: The unordered structure increases concomitant with a decrease in the remaining structure, thus, revealing breakdown of the intact protein into smaller fragments in an open reaction system such as the stomach.
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A Soluble Fragment of the Tumor Antigen BCL2-associated Athanogene 6 (BAG-6) Is Essential and Sufficient for Inhibition of NKp30 Receptor-dependent Cytotoxicity of Natural Killer Cells

TL;DR: This study gives the first molecular insights into BAG-6-mediated inhibition of NKp30-dependent NK cell cytotoxicity as part of a tumor immune escape mechanism and provides an access point to restore tumor immunosurveillance by NK cells and to increase the efficacy of cellular therapies.
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Lipid-Protein Interactions in the Regulated Betaine Symporter BetP Probed by Infrared Spectroscopy *

TL;DR: A regulation mechanism in which lipid-protein interactions, especially with the C-terminal domain and the functional important gating helices transmembrane helice 3 (TMH3) and TMH12, confine BetP to its down-regulated transport state is suggested.