کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2076551 | 1079453 | 2008 | 9 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Protein crystal's shape and polymorphism prediction within the limits resulting from the exploration of the Miyazawa-Jernigan matrix
دانلود مقاله + سفارش ترجمه
دانلود مقاله ISI انگلیسی
رایگان برای ایرانیان
کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
ریاضیات
مدلسازی و شبیه سازی
پیش نمایش صفحه اول مقاله

چکیده انگلیسی
A computer study of the prediction of the protein crystal's shape and polymorphism of crystal's structures within the limits resulting from the exploration of the Miyazawa-Jernigan matrix is presented. In this study, a coarse-graining procedure was applied to prepare a two-dimensional growth unit, where instead of full atom representation of the protein a two-type (hydrophobic-hydrophilic, HP) aminoacidal representation was used. The interaction energies between hydrophobic (EHH) aminoacids were chosen from the well-known HP-type models (EHHâ[â4,â3,â2.3,â1]), whereas interaction energies between hydrophobic and hydrophilic aminoacids (EHP) as well as interaction energies between hydrophilic aminoacids (EPP) were chosen from the range: <â1,1>, but not all values from this range fulfiled limitations resulting from the exploration of the Miyazawa-Jernigan matrix. Exploring every positively vetted combinations of energy interactions a polymorphism of the unit cell was observed what led to the fact that different final crystal's shapes were obtained.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biosystems - Volume 94, Issue 3, December 2008, Pages 233-241
Journal: Biosystems - Volume 94, Issue 3, December 2008, Pages 233-241
نویسندگان
Jacek Siódmiak,