101 - 120 toradh á dtaispeáint as 29,385 toradh san iomlán ar an gcuardach 'form is (((((remote. OR evolveddsssdss.) OR resolved.) OR involves.) OR involved.) OR resolve.)*', am iarratais: 0.74s Beachtaigh na torthaí
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    Growth Kinetics of Polyelectrolyte Complexes Formed from Oppositely-Charged Homopolymers Studied by Time-Resolved Ultra-Small-Angle X‑ray Scattering de réir Rintaro Takahashi (1513495)

    Foilsithe / Cruthaithe 2017
    “…We have monitored the kinetic process of polyelectrolyte complex formation between sodium polyacrylate (SPA) and polyallylamine hydrochrolide (PAH) in aqueous NaCl solution by time-resolved ultra-small-angle X-ray scattering (TR-USAXS) combined with rapid mixing. …”
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  11. 111

    Monotropic Transition Mechanism of <i>m</i>‑Hydroxybenzoic Acid Investigated by Temperature-Resolved Second Harmonic Generation de réir Simon Clevers (1584676)

    Foilsithe / Cruthaithe 2013
    “…Temperature-resolved second harmonic generation (TR-SHG) and SHG microscopy were used to study under normal pressure the solid–solid transition mechanism occurring between the two monotropically related polymorphic forms (metastable <i>Pna</i>2<sub>1</sub> and stable <i>P</i>2<sub>1</sub>/<i>n</i>) of 3-hydroxybenzoic acid (MHBA). …”
  12. 112

    Monotropic Transition Mechanism of <i>m</i>‑Hydroxybenzoic Acid Investigated by Temperature-Resolved Second Harmonic Generation de réir Simon Clevers (1584676)

    Foilsithe / Cruthaithe 2013
    “…Temperature-resolved second harmonic generation (TR-SHG) and SHG microscopy were used to study under normal pressure the solid–solid transition mechanism occurring between the two monotropically related polymorphic forms (metastable <i>Pna</i>2<sub>1</sub> and stable <i>P</i>2<sub>1</sub>/<i>n</i>) of 3-hydroxybenzoic acid (MHBA). …”
  13. 113
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  17. 117

    Dopamine transporter oligomerization involves the scaffold domain, but spares the bundle domain de réir Kumaresan Jayaraman (1332030)

    Foilsithe / Cruthaithe 2018
    “…It has been shown that hDAT and other members of the monoamine transporter family exist in oligomeric forms at the plasma membrane. Several residues are known to be involved in oligomerization, but interaction interfaces, oligomer orientation and the quarternary arrangement in the plasma membrane remain poorly understood. …”
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