V
Viktor Hornak
Researcher at Stony Brook University
Publications - 28
Citations - 8306
Viktor Hornak is an academic researcher from Stony Brook University. The author has contributed to research in topics: Rhodopsin & HIV-1 protease. The author has an hindex of 22, co-authored 26 publications receiving 7595 citations. Previous affiliations of Viktor Hornak include Brookhaven National Laboratory.
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Journal ArticleDOI
Comparison of multiple Amber force fields and development of improved protein backbone parameters.
Viktor Hornak,Robert Abel,Asim Okur,Bentley Strockbine,Adrian E. Roitberg,Carlos Simmerling,Carlos Simmerling +6 more
TL;DR: An effort to improve the φ/ψ dihedral terms in the ff99 energy function achieves a better balance of secondary structure elements as judged by improved distribution of backbone dihedrals for glycine and alanine with respect to PDB survey data.
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HIV-1 protease flaps spontaneously open and reclose in molecular dynamics simulations
TL;DR: The data strongly support the hypothesis that the unliganded protease predominantly populates the semiopen conformation, with closed and fully open structures being a minor component of the overall ensemble.
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Crystallographic structure of the K intermediate of bacteriorhodopsin: conservation of free energy after photoisomerization of the retinal.
TL;DR: The K state, an early intermediate of the bacteriorhodopsin photocycle, is produced in crystals in a photostationary state at 100K, with 40% yield, and its X-ray diffraction structure is determined to 1.43 A resolution.
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Helix movement is coupled to displacement of the second extracellular loop in rhodopsin activation.
Shivani Ahuja,Viktor Hornak,Elsa C. Y. Yan,Elsa C. Y. Yan,Natalie Syrett,Joseph A. Goncalves,Amiram Hirshfeld,Martine Ziliox,Thomas P. Sakmar,Mordechai Sheves,Philip J. Reeves,Steven O. Smith,Markus Eilers +12 more
TL;DR: NMR measurements reveal that structural changes in EL2 are coupled to the motion of helix H5 and breaking of the ionic lock that regulates activation in this prototypical G protein–coupled receptor.
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Location of Trp265 in metarhodopsin II : Implications for the activation mechanism of the visual receptor rhodopsin
Evan Crocker,Markus Eilers,Shivani Ahuja,Viktor Hornak,Amiram Hirshfeld,Mordechai Sheves,Steven O. Smith +6 more
TL;DR: Solid-state magic angle spinning NMR measurements are presented that support the proposal that interaction of Trp 265 with the retinal chromophore is responsible for stabilizing an inactive conformation in the dark, and that motion of the beta-ionone ring allows Trp265(6.48) and transmembrane helix H6 to adopt active conformations in the light.