کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
5189422 | 1381184 | 2006 | 13 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Analysis of cation-Ï interactions to the structural stability of RNA binding proteins
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کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی آلی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
Cation-Ï interactions play an important role to the stability of protein structures. In this work, we have analyzed the influence of cation-Ï interactions in RNA binding proteins. We observed cation-Ï interactions in 32 out of 51 RNA binding proteins and there is a strong correlation between the number of amino acid residues and number of cation-Ï interactions. The analysis on the influence of short (<±3 residues), medium (±3 or ±4 residues) and long range contacts (>±4 residues) showed that the cation-Ï interactions are mainly formed by long-range contacts. The cation-Ï interaction energy for Arg-Trp is found to be the strongest among all interacting pairs. Analysis on the preferred secondary structural conformation of the residues involved in cation-Ï interaction indicates that the cationic Lys and Arg prefer to be in α-helices and β-strands, respectively, whereas the aromatic residues prefer to be in strand and coil regions. Most of the cation-Ï interactions forming residues in RNA binding proteins are conserved among homologous sequences. Further, the cation-Ï interactions have distinct roles to the stability of RNA binding proteins in addition to other conventional non-covalent interactions. The results observed in the present study will be useful in understanding the contribution of cation-Ï interactions to the stability of RNA binding proteins.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Polymer - Volume 47, Issue 2, 13 January 2006, Pages 709-721
Journal: Polymer - Volume 47, Issue 2, 13 January 2006, Pages 709-721
نویسندگان
S. Chakkaravarthi, M. Michael Gromiha,