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Hekmat, A.,Saboury, A. A.,Divsalar, A.,Khanmohammadi, M. Korean Chemical Society 2008 Bulletin of the Korean Chemical Society Vol.29 No.8
Results of intrinsic and extrinsic fluorescence studies on choline oxidase revealed that the enzyme at high alkaline pH values has more accessible hydrophobic patches relative to acidic pH. Fluorescence quenching studies with acrylamide confirm these changes. The quenching constants were also determined at different pH(s) by using the Stern-Volmer equation. CD studies showed that at higher pH a transition from $\alpha$-helix to $\beta$- structure was appeared while at lower pH the content of $\alpha$-helix structure was increased. Furthermore, analysis of the spectral data using chemometric method gave evidence for existence of intermediate components at very high pH(s). Results of thermal denaturation evaluated that the enzyme has the most instability at higher pH(s). Altogether low and high pH values caused significant alteration on secondary and tertiary structures of choline oxidase via inducing of an intermediate.
A. Hekmat, A. A. Saboury,A. Divsalar,M. Khanmohammadi 대한화학회 2008 Bulletin of the Korean Chemical Society Vol.29 No.8
Results of intrinsic and extrinsic fluorescence studies on choline oxidase revealed that the enzyme at high alkaline pH values has more accessible hydrophobic patches relative to acidic pH. Fluorescence quenching studies with acrylamide confirm these changes. The quenching constants were also determined at different pH(s) by using the Stern-Volmer equation. CD studies showed that at higher pH a transition from α-helix to β- structure was appeared while at lower pH the content of α-helix structure was increased. Furthermore, analysis of the spectral data using chemometric method gave evidence for existence of intermediate components at very high pH(s). Results of thermal denaturation evaluated that the enzyme has the most instability at higher pH(s). Altogether low and high pH values caused significant alteration on secondary and tertiary structures of choline oxidase via inducing of an intermediate.
S.A. Safwan,Assma Saleh,Hekmat M. Hassanein,Nagwa El Meshed 한국물리학회 2018 Current Applied Physics Vol.18 No.1
The hydrostatic pressure (P) influence of the degenerate energy states inside an inverse parabolic quantum dot (IPQD), with and without an external magnetic field, was performed within the frame of the effective mass approximation. Our theoretical results showed that the effect of relatively high pressure clearly appeared to induce a crossing between the excited states in the strong confinement region. But in the weak confinement region, such crossing disappeared and, in addition, the excited states got reordered. In the presence of an external magnetic field the hydrostatic pressure modified the crossing points of the degenerate states. We investigated the electron-heavy hole transition energy. It displayed a blue shift with increasing the pressure values and the magnetic field strength. But it showed an adhesive red shift by increasing the IPQD size.