کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1926144 | 1536443 | 2010 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
The conformation of end-groups is one determinant of carotenoid topology suitable for high fidelity molecular recognition: A study of β- and ε-end-groups
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
Conformation affects a carotenoid's ability to bind selectively to proteins. We calculated adiabatic energy profiles for rotating the ring end-groups around the C6C7 bond and for flexing of the ring with respect to the polyene chain. The choice of computational methods is important. A low, 4.2 kcal/mol barrier to rotation exists for a β-ring. An 8.3 kcal/mol barrier exists for rotation of an ε-ring. Rotation of the ε-ring is sensitive to substitution at C3. In the absence of external forces neither β- nor ε-rings are rotationally constrained. The nearly parallel alignment of the β-ring to the C6C7 bond axis contrasts to the more perpendicular orientation of the ε-ring. Flexion of a β-ring to the minimized ε-ring conformation requires â¼23 kcal/mol; extension of the ε-ring to the minimized β-ring conformation requires â¼8 kcal/mol. Selectivity associated with β- versus ε-rings is dominated by the inability of the β-ring to flex to minimize protein/ring steric interactions and maximize van der Waal's attractions with the binding site.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Archives of Biochemistry and Biophysics - Volume 493, Issue 2, 15 January 2010, Pages 169-174
Journal: Archives of Biochemistry and Biophysics - Volume 493, Issue 2, 15 January 2010, Pages 169-174
نویسندگان
John T. Landrum, David C. Chatfield, Alex M. Mebel, Francesca Alvarez-Calderon, Melissa V. Fernandez,