A Miniature Protein Stabilized by a Cation-π Interaction Network.
A Miniature Protein Stabilized by a Cation-π Interaction Network.
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DOI：
10.1021/jacs.5b10285
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发表时间：
2016-02-10
影响因子：
15
通讯作者：
Kirshenbaum K
中科院分区：
文献类型：
--
作者：
Craven TW;Cho MK;Traaseth NJ;Bonneau R;Kirshenbaum K
The design of folded miniature proteins is predicated on establishing non-covalent interactions that direct the self-assembly of discrete thermo-stable tertiary structures. In this work, we describe how a network of cation-π interactions present in proteins containing “WSXWS motifs” can be emulated to stabilize the core of a miniature protein. This 19-residue protein sequence recapitulates a set of interdigitated arginine and tryptophan residues that stabilize a distinctive β-strand:loop:PPII-helix topology. Validation of the compact fold determined by NMR was carried out by mutagenesis of the cation-π network and by comparison to the corresponding disulfide-bridged structure. These results support the involvement of a coordinated set of cation-π interactions that stabilize the tertiary structure.
