Close pairs of carboxylates: a possibility of multicenter hydrogen bonds in proteins.
Close pairs of carboxylates: a possibility of multicenter hydrogen bonds in proteins.
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紧密的羧酸盐对：蛋白质中多中心氢键的可能性。
DOI：
10.1093/proeng/gzg027
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发表时间：
2003
期刊：
影响因子：
--
通讯作者：
Weber,IreneT
中科院分区：
文献类型：
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作者：
Torshin,IvanY;Harrison,RobertW;Weber,IreneT
氢与供体原子的共价附着可能不是稳定氢键的基本特征。带正电的粒子（如质子）位于两个带负电的残基之间，可能导致两个带负电的残基之间稳定的相互作用。本文分析了大量蛋白质链中Asp-Glu对的紧密残基；鉴定出840对这样的残基，其中28%是由金属离子稳定的，12%是由附近的正电残基稳定的，60%可能是由质子稳定的。羧酸对中没有明显的结构约束、二级结构偏好、较低的b因子以及pH值与最小O-O距离之间的明显相关性表明，大多数异常接近的对确实可以通过共享质子来稳定。讨论了蛋白质稳定性和建模的意义。
Covalent attachment of hydrogen to the donor atom may be not an essential characteristic of stable hydrogen bonds. A positively charged particle (such as a proton), located between the two negatively charged residues, may lead to a stable interaction of the two negative residues. This paper analyzes close Asp–Glu pairs of residues in a large set of protein chains; 840 such pairs of residues were identified, of which 28% were stabilized by a metal ion, 12% by a positive residue nearby and 60% are likely to be stabilized by a proton. The absence of apparent structural constraints, secondary structure preferences, somewhat lowerB-factors and a distinct correlation between pH and the minimal O–O distance in carboxylate pairs suggest that most of the abnormally close pairs could indeed be stabilized by a shared proton. Implications for protein stability and modeling are discussed.