Side chain flexibility and the symmetry of protein homodimers

Yaffa Shalit, Inbal Tuvi-Arad

نتاج البحث: نشر في مجلةمقالةمراجعة النظراء


A comprehensive analysis of crystallographic data of 565 high-resolution protein homodimers comprised of over 250,000 residues suggests that amino acids form two groups that differ in their tendency to distort or symmetrize the structure of protein homodimers. Residues of the first group tend to distort the protein homodimer and generally have long or polar side chains. These include: Lys, Gln, Glu, Arg, Asn, Met, Ser, Thr and Asp. Residues of the second group contribute to protein symmetry and are generally characterized by short or aromatic side chains. These include: Ile, Pro, His, Val, Cys, Leu, Trp, Tyr, Phe, Ala and Gly. The distributions of the continuous symmetry measures of the proteins and the continuous chirality measures of their building blocks highlight the role of side chain geometry and the interplay between entropy and symmetry in dictating the conformational flexibility of proteins.

اللغة الأصليةالإنجليزيّة
رقم المقالe0235863
دوريةPLoS ONE
مستوى الصوت15
رقم الإصدار7 July
المعرِّفات الرقمية للأشياء
حالة النشرنُشِر - يوليو 2020

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Copyright © 2020 Shalit, Tuvi-Arad.


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