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Browsing WOS by WoS Q "Q3"

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    Journal Article
    Citation - WoS: 3
    Exactly solvable madelung fluid and complex burgers equations: a quantum sturm-liouville connection
    (Springer, 2012) Buyukasik, Sirin A.; Pashaev, Oktay K.
    Quantum Sturm-Liouville problems introduced in our paper (BuyukaAYA +/- k et al. in J Math Phys 50:072102, 2009) provide a reach set of exactly solvable quantum damped parametric oscillator models. Based on these results, in the present paper we study a set of variable parametric nonlinear Madelung fluid models and corresponding complex Burgers equations, related to the classical orthogonal polynomials of Hermite, Laguerre and Jacobi types. We show that the nonlinear systems admit direct linearazation in the form of Schrodinger equation for a parametric harmonic oscillator, allowing us to solve exactly the initial value problems for these equations by the linear quantum Sturm-Liouville problem. For each type of equations, dynamics of the probability density and corresponding zeros, as well as the complex velocity field and related pole singularities are studied in details.
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    Journal Article
    Citation - WoS: 5
    Heme binding constricts the conformational dynamics of the cytochrome: Heme binding cavity
    (Amer Chemical Soc, 2012) Akdogan, Yasar; Anbazhagan, Veerappan; Hinderberger, Dariush; Schneider, Dirk
    Cytochrome b(559)' is a transmembrane protein formed by homodimerization of the 44-residue PsbF polypeptide and noncovalent binding of a heme cofactor. The PsbF polypeptide can dimerize in the absence and presence of heme. To monitor structural alterations associated with binding of heme to the apocytochrome, we analyzed the apo- and holo-cytochrome structure by electron paramagnetic resonance spectroscopy. Spin labeling of amino acids located close to the heme binding domain of the cytochrome revealed that the structure of the heme binding domain is unconstrained in the absence of heme. Heme binding restricts the conformational dynamics of the heme binding domain, resulting in the structurally more constricted holo-cytochrome structure.