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Hydrogen bonds with pi-acceptors in proteins: Frequencies and role instabilizing local 3D structures

机译:蛋白质中pi受体的氢键:频率和稳定局部3D结构的作用

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A comprehensive structural analysis of X-H . . . pi hydrogen bonding in proteins is performed based on 592 published high-resolution crystal structures (less than or equal to 1.6 Angstrom). All potential donors and accepters are considerered, including acidic C-H groups. The sample contains 1311 putative X-H . . . pi hydrogen bonds with N-H, O-H or S-H donors, that is about one per 10.8 aromatic residues. By far the most efficient n-acceptor is the side-chain of Trp, which accepts one X-H . . . pi hydrogen bond per 5.7 residues. The focus of the analysis is on recurrent structural patterns involving regular secondary structure elements. Numerous examples are found where peptide X-H . . . pi interactions are functional in stabilization of helix termini, strand ends, strand edges, beta -bulges and regular turns. Side-chain X-H . . . pi hydrogen bonds are formed in considerable numbers in alpha -helices and beta -sheets. Geometrical data on various types of X--H . . . pi hydrogen bonds are given.
机译:X-H的综合结构分析。 。 。蛋白质中的pi氢键是基于592个已公开的高分辨率晶体结构(小于或等于1.6埃)进行的。考虑了所有潜在的供体和受体,包括酸性C-H基团。该样本包含1311个推定的X-H。 。 。 π氢与N-H,O-H或S-H供体键合,大约每10.8个芳族残基一个。到目前为止,最有效的n受体是Trp的侧链,它可以接受一个X-H。 。 。每5.7个残基有pi氢键。分析的重点是涉及常规二级结构元素的循环结构模式。发现许多例子,其中肽X-H。 。 。 pi相互作用在稳定螺旋末端,链末端,链边缘,β-凸出和规则的转弯中起作用。侧链X-H。 。 。在α-螺旋和β-折叠中形成大量的π氢键。各种X–H的几何数据。 。 。给出了π氢键。

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