HYDROGEN-BONDING IN GLOBULAR-PROTEINS
HYDROGEN-BONDING IN GLOBULAR-PROTEINS
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DOI：
10.1016/0022-2836(92)91058-w
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发表时间：
1992-08-20
影响因子：
5.6
通讯作者：
ROSE, GD
中科院分区：
文献类型：
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作者：
STICKLE, DF;PRESTA, LG;ROSE, GD
对 42 个 X 射线阐明的蛋白质中的氢键进行了全球普查，并确定了以下人口统计趋势：（1）大多数氢键是局部的，即在顺序接近的伙伴之间，主要的例外是氢键离子对。 (2)大多数氢键位于蛋白质的主链原子之间，平均为68%。 (3)所有研究的蛋白质都具有广泛的氢键二级结构，平均为82%。 (4)几乎所有主链氢键都在二级结构的单个元素内。近似三分法则适用：略多于三分之一（37％）的形成→i→3个氢键，几乎三分之一（32％）形成→i→4个氢键，略少于三分之一（26％）存在于成对的β-折叠链中。其余 5% 并不完全位于单个螺旋、圈或片内。 (5)侧链至主链的氢键聚集在螺旋封端位置。 (6) 螺旋中存在广泛的氢键作用。 (7) 近似地，氢键总数是蛋白质螺旋和片层含量的简单函数。 (8) 一个独特的数量，称为氢键减少数，定义为当每个供体：受体对被限制为 1:1 时可能存在的最大氢键数量。该数量与链长呈线性关系，每个残基减少 0·71 个氢键。讨论了这些结果对蛋白质折叠途径的影响。
A global census of the hydrogen bonds in 42 X-ray-elucidated proteins was taken and the following demographic trends identified: (1) Most hydrogen bonds are local, i.e. between partners that are close in sequence, the primary exception being hydrogen-bonded ion pairs. (2) Most hydrogen bonds are between backbone atoms in the protein, an average of 68%. (3) All proteins studied have extensive hydrogen-bonded secondary structure, an average of 82%. (4) Almost all backbone hydrogen bonds are within single elements of secondary structure. An approximate rule of thirds applies: slightly more than one-third (37%) formi→i→ 3 hydrogen bonds, almost one-third (32%) form →i→ 4 hydrogen bonds, and slightly less than one-third (26%) reside in paired strands of β-sheet. The remaining 5% are not wholly within an individual helix, turn or sheet. (5) Side-chain to backbone hydrogen bonds are clustered at helix-capping positions. (6) An extensivenerworkof hydrogen bonds is present in helices. (7) To a close approximation, the total number of hydrogen bonds is a simple function of a protein'e helix and sheet content. (8) A unique quantity, termed thereducednumber of hydrogen bonds, is defined as the maximum number of hydrogen bonds possible when every donor: acceptor pair is constrained to be 1:1. This quantity scales linearly with chain length, with 0·71 reduced hydrogen bond per residue. Implications of these results for pathways of protein folding are discussed.