H
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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Journal ArticleDOI
Multimode, cooperative mechanism of action of allosteric HIV-1 integrase inhibitors.
Jacques J. Kessl,Nivedita Jena,Yasuhiro Koh,Humeyra Taskent-Sezgin,Alison Slaughter,Lei Feng,Suresh de Silva,Li Wu,Stuart F. J. Le Grice,Alan Engelman,James R. Fuchs,Mamuka Kvaratskhelia +11 more
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.
Journal ArticleDOI
Azidohomoalanine: A Conformationally Sensitive IR Probe of Protein Folding, Protein Structure, and Electrostatics
Humeyra Taskent-Sezgin,Juah Chung,Partha S. Banerjee,Sureshbabu Nagarajan,R. Brian Dyer,Isaac S. Carrico,Daniel P. Raleigh +6 more
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.
Journal ArticleDOI
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.
Humeyra Taskent-Sezgin,Juah Chung,Vadim Patsalo,Shigeki J. Miyake-Stoner,Andrew M. Miller,Scott H. Brewer,Ryan A. Mehl,David F. Green,Daniel P. Raleigh,Isaac S. Carrico +9 more
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.
Journal ArticleDOI
Modulation of p-Cyanophenylalanine Fluorescence by Amino Acid Side-chains and Rational Design of Fluorescence Probes of α-Helix Formation
Humeyra Taskent-Sezgin,Peter Marek,Rosanne Thomas,Daniel Goldberg,Juah Chung,Isaac S. Carrico,Daniel P. Raleigh +6 more
TL;DR: The quenching of p-cyanophenylalanine fluorescence by specific side chains is exploited in developing specific, high-sensitivity, fluorescence probes of helix formation.
Journal ArticleDOI
Differential ordering of the protein backbone and side chains during protein folding revealed by site-specific recombinant infrared probes.
Sureshbabu Nagarajan,Humeyra Taskent-Sezgin,Dzmitry Parul,Isaac S. Carrico,Daniel P. Raleigh,R. Brian Dyer +5 more
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.