Reuben Hiller
Tel Aviv University
36 Papers
254 Citations
Reuben Hiller is an academic researcher from Tel Aviv University. The author has contributed to research in topics: Sodium-calcium exchanger & Chemistry. The author has an hindex of 15, co-authored 33 publications. Previous affiliations of Reuben Hiller include University of Maryland Biotechnology Institute & Weizmann Institute of Science.
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Papers
Induced peptide conformations in different antibody complexes: molecular modeling of the three-dimensional structure of peptide-antibody complexes using NMR-derived distance restraints.
TL;DR: Intramolecular interactions in bound cholera toxin peptide (CTP3) in three antibody complexes were studied by two-dimensional transferred NOE spectroscopy and revealed a relationship between amino acid sequence and combining site structure and function.
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Solution conformation of a peptide corresponding to the principal neutralizing determinant of HIV-1IIIB: a two-dimensional NMR study.
TL;DR: The 24 amino acid peptide RP135 corresponds in its amino acid sequence to the principal neutralizing determinant (PND) of the IIIB isolate of HIV-1 and a helical conformation was found to be stabilized by the addition of TFE, while no nascent helix conformations could be observed in the N-terminal part of RP135 in water, however, nascent helIX conformations were not observed in aqueous solutions of RP142.
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Asymmetric Preorganization of Inverted Pair Residues in the Sodium-Calcium Exchanger.
Moshe Giladi,Lior Almagor,Liat van Dijk,Reuben Hiller,Petr Man,Eric Forest,Eric Forest,Daniel Khananshvili +7 more
TL;DR: The present data strongly support the idea that asymmetric preorganization of the ligand-free ion-pocket predefines catalytic reorganization of ion-bound residues, where secondary interactions with adjacent residues couple the alternating access in NCX and similar proteins.
Cooperativity among manganese-binding sites in the H+-ATPase of chloroplasts.
Reuben Hiller,Chanoch Carmeli +1 more
TL;DR: Coupling factor, isolated from lettuce chloroplasts, contained several binding sites for Mn2+ ions that showed strong cooperative interactions, and it is suggested that the cooperative interaction among the Mn2-binding sites is an expression of the interaction between the active sites of the enzyme which is required for catalysis.
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Population shift underlies Ca2+-induced regulatory transitions in the sodium-calcium exchanger (NCX).
TL;DR: Ca2+-induced population shift governs NCX activation with no significant contribution of global conformational changes in CBD alignment and ensemble optimization method SAXS analysis demonstrates that the apo and Mg2-bound forms of CBD12 are highly flexible, whereas Ca2+ binding to the Ca3–Ca4 sites results in a population shift of conformational landscape to more rigidified states.
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