Author

O. Gocenler

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biochemistry· 2 Biophysics· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:differential expression· 1 Research Focus:drug response / drug discovery· 1 Assay:metabolomics· 1 Approach:microscopy & imaging analysis· 1 Research Focus:protein folding & dynamics· 1 Assay:protein structure· 1 Approach:statistical model· 1

Frequent Co-Authors

C. Dag· 4 shared K. Kahraman· 3 shared C. Buyukdag· 2 shared C. M. Yenici· 2 shared A. B. Peksen· 1 shared A. Barty· 1 shared A. Batyuk· 1 shared A. D. Yucel· 1 shared

Activity by Year

2020-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 29 mutual co-author links

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4 shared papersBiochemistry

C. Dag

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

Characterization of Turkish Pine Honey and Differentiation from Floral Honeys by NMR Spectroscopy and Chemometric Analysis

K. Kahraman, O. Gocenler, C. Dag

This study uses NMR spectroscopy and chemometric analysis to distinguish Turkish Pine honey from other floral honeys based on unique chemical profiles.

bioRxiv · Sep 5, 2023Biochemistry

Characterizing the monomer-dimer equilibrium of UbcH8/Ube2L6: A combined SAXS and NMR study

K. Kahraman, S. A. Robson, O. Gocenler, C. M. Yenici, C. D. Tozkoparan, J. M. Klein, V. Dötsch, E. S. Elgin, A. L. Haas, J. J. Ziarek, C. Dag

This study uses SAXS and NMR to show UbcH8 exists in a concentration-dependent monomer-dimer equilibrium with dimerization affecting E1 and E3 interfaces.

bioRxiv · Apr 13, 2023Biochemistry

Biomolecular solution X-ray scattering at n2STAR Beamline

O. Gocenler, C. M. Yenici, K. Kahraman, C. Buyukdag, C. Dag

The paper evaluates home source SAXS data collection and optimization for generating viable structural models of biomolecules.

bioRxiv · May 20, 2022Biophysics

Near-Physiological-Temperature Serial Femtosecond X-ray Crystallography Reveals Novel Conformations of SARS-CoV-2 Main Protease Active Site for Improved Drug Repurposing

S. Durdagi, C. Dag, B. Dogan, M. Yigin, T. Avsar, C. Buyukdag, I. Erol, F. B. Ertem, S. Calis, G. Yildirim, M. Orhan, O. Guven, B. Aksoydan, E. Destan, K. Sahin, , Sn

The paper determines two apo structures of SARS-CoV-2 main protease at near-physiological temperature using SFX and uses molecular simulations to analyze inhibitor binding for drug repurposing.

bioRxiv · Sep 9, 2020Biophysics