Showing 1 - 7 results of 7 for search '(( 5 i decrease ) OR ((( _ e decrease ) OR ( _ bind decrease ))))~', query time: 0.13s Refine Results
  1. 1

    Tailoring optical absorption in silicon nanostructures from UV to visible light: A TDDFT study by Hassan, Walid M.I.

    Published 2016
    “…(ii) The exciton binding energy is seen to decrease by approximately 45% from 0.67 eV to about 0.3 eV with length increase, for a nanostructure with a cross-section diameter of approximately 12 Å. …”
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  2. 2

    A computational approach for investigating the mutational landscape of RAC-alpha serine/threonine-protein kinase (AKT1) and screening inhibitors against the oncogenic E17K mutation... by Thirumal Kumar, D

    Published 2019
    “…The molecular interaction study also revealed that the co-crystallized AKT1 inhibitor N-(4-(5-(3-acetamidophenyl)-2-(2-aminopyridin-3-yl)-3H-imidazo [4,5-b]pyridin-3-yl)benzyl)-3-fluorobenzamide (12j) exhibited a better interaction with native AKT1 compared with the E17K mutant AKT1 protein, whereas, Akti-1/2 exhibited the opposite effects, i.e., a better interaction with the E17K mutant AKT1 than the native AKT1. …”
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  3. 3

    Divergent Biochemical Properties and Disparate Impact of Arrhythmogenic Calmodulin Mutations on Zebrafish Cardiac Function by Da'as, Sahar I.

    Published 2024
    “…We recently showed that four arrhythmogenic CaM mutations (N98I, D132E, D134H, and Q136P) significantly reduce the binding of CaM to RyR2. …”
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    Enzymatic treatment of peanut butter to reduce the concentration of major peanut allergens by Yu, Jianmei

    Published 2013
    “…Treatment of peanut butter with a combination of trypsin and alpha-chymotrypsin resulted in a decrease in IgE-binding, suggesting that enzymatic treatment has the potential to reduce the allergenicity. …”
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  6. 6

    Calmodulin Mutations Associated with Congenital Cardiac Disease Display Novel Biophysical and Biochemical Characteristics by Nomikos, Michail

    Published 2018
    “…In contrast, in the presence of Ca2+, there was a significant decrease in the stability of the five proteins following the order CaMWT> CaMN98I > CaMD132E > CaMQ136P > CaMD134H. …”
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