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Humeyra Taskent-Sezgin

Researcher at Stony Brook University

Publications -  6
Citations -  444

Humeyra Taskent-Sezgin is an academic researcher from Stony Brook University. The author has contributed to research in topics: Protein folding & Cooperativity. The author has an hindex of 6, co-authored 6 publications receiving 409 citations. Previous affiliations of Humeyra Taskent-Sezgin include National Institutes of Health & Ohio State University.

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Multimode, cooperative mechanism of action of allosteric HIV-1 integrase inhibitors.

TL;DR: 2-(quinolin-3-yl) acetic acid derivatives impairs both integrase-LEDGF binding and LEDGF-independent integrase catalytic activities with similar IC50 values, defining them as bona fide allosteric inhibitors of integrase function.
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Azidohomoalanine: A Conformationally Sensitive IR Probe of Protein Folding, Protein Structure, and Electrostatics

TL;DR: It is shown that an azido-bearing nonnatural amino acid, azidohomoalanine (Aha), provides a high-sensitivity probe of protein structure, protein folding, and protein electrostatics.
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Interpretation of p-cyanophenylalanine fluorescence in proteins in terms of solvent exposure and contribution of side-chain quenchers: a combined fluorescence, IR and molecular dynamics study.

TL;DR: Analysis of mutant proteins and model peptides demonstrates that the reduced native state fluorescence is caused by the effective quenching of p-cyanophenylalanine fluorescence via FRET to tyrosine side-chains.
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Modulation of p-Cyanophenylalanine Fluorescence by Amino Acid Side-chains and Rational Design of Fluorescence Probes of α-Helix Formation

TL;DR: The quenching of p-cyanophenylalanine fluorescence by specific side chains is exploited in developing specific, high-sensitivity, fluorescence probes of helix formation.
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Differential ordering of the protein backbone and side chains during protein folding revealed by site-specific recombinant infrared probes.

TL;DR: It is found that side-chain ordering in a key region of the β-sheet structure occurs on a slower time scale than ordering of the backbone during the folding of NTL9, likely as a result of the transient formation of non-native side- chain interactions.