We demonstrate in this contribution the evidence that significant cooperative binding effect can be identified for the amino acid sites that are determinant to the binding characteristics in peptide–peptide interactions. The analysis of tryptophan‐scanning mutagenesis of the 14‐mer peptide consisting only of glycine provides a mapping of position‐dependent contributions to the binding energy. The pronounced tryptophan‐associated peptide–peptide interactions are originated from the indole moieties with the main chains of 14‐mer glycines containing N–H and CO moieties. Specifically, with the presence of two tryptophans as determinant amino acids, cooperative binding can be observed, which are dependent on relative positions of the two tryptophans with a “volcano”‐like characteristics. An optimal separation of 6–10 amino acids between two adjacent binding sites can be identified to achieve maximal binding interactions.

中文翻译：

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色氨酸扫描诱变揭示了位置编码的多价肽-肽相互作用。

我们证明了这一证据，可以确定对于决定肽-肽相互作用中结合特征的氨基酸位点具有明显的协同结合作用。仅由甘氨酸组成的14-mer肽的色氨酸扫描诱变分析提供了位置依赖性对结合能的贡献图。色氨酸相关的肽-肽相互作用明显是由吲哚基团与包含NH和CO基团的14-聚甘氨酸的主链形成的。特别是，当存在两个色氨酸作为决定性氨基酸时，可以观察到协同结合，这取决于具有“火山”状特征的两个色氨酸的相对位置。