کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
5374346 | 1504261 | 2012 | 8 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
A QM/MM-MD study on protein electronic properties: Circular dichroism spectra of oxytocin and insulin
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کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی تئوریک و عملی
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چکیده انگلیسی
A QM/MM (quantum-mechanical/molecular-mechanical) molecular-dynamics approach based on the generalized hybrid-orbital (GHO) method, in conjunction with the second-order perturbation (MP2) theory and the second-order approximate coupled-cluster (CC2) model, is employed to calculate electronic property accounting for a protein environment. Circular dichroism (CD) spectra originating from chiral disulfide bridges of oxytocin and insulin at room temperature are computed. It is shown that the sampling of thermal fluctuation of molecular geometries facilitated by the GHO-MD method plays an important role in the obtained spectra. It is demonstrated that, while the protein environments in an oxytocin molecule have significant electrostatic influence on its chiral center, it is compensated by solvent induced charges. This gives a reasonable explanation to experimental observations. GHO-MD simulations starting from different experimental structures of insulin indicate that existence of the disulfide bridges with negative dihedral angles is crucial.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Chemical Physics - Volume 401, 5 June 2012, Pages 95-102
Journal: Chemical Physics - Volume 401, 5 June 2012, Pages 95-102
نویسندگان
Yuya Kitagawa, Yoshinobu Akinaga, Yukio Kawashima, Jaewoon Jung, Seiichiro Ten-no,