کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
443698 692752 2012 7 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
A dynamical approach to contact distance based protein structure determination
موضوعات مرتبط
مهندسی و علوم پایه شیمی شیمی تئوریک و عملی
پیش نمایش صفحه اول مقاله
A dynamical approach to contact distance based protein structure determination
چکیده انگلیسی

Protein native structure topology based folding dynamics captures many aspects of protein folding. The fact that folding is driven by a potential derived only from residue pairs in native contact, a sparse distance matrix, lead us to postulate this as a solution method to the molecular distance geometry problem. In the standard Go model non-bonded residues move under the influence of a Lennard–Jones potential and consequently folding is slow. In this study we apply a faster quadratic potential Go model to solving the full-atom distance geometry problem, where distance data is based only on residue atoms within 5 Å in the native structure. We show that the method works well when only atomic contact data is known and when a substantial proportion of this contact data is missing. Also, we show that the method can be applied in conjunction with secondary structure prediction schemes to enhance accuracy in cases of missing contact data.

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ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Molecular Graphics and Modelling - Volume 32, February 2012, Pages 75–81
نویسندگان
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