Quantitating amino acid beta-strand preferences, turn propensities and cross-strand interactions in a designed hairpin peptide.
Quantitating amino acid beta-strand preferences, turn propensities and cross-strand interactions in a designed hairpin peptide.
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定量设计的发夹肽中的氨基酸 β 链偏好、转向倾向和跨链相互作用。
DOI：
10.1007/978-0-387-73657-0_31
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发表时间：
2009
影响因子：
--
通讯作者：
Andersen,NielsH
中科院分区：
文献类型：
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作者：
Huggins,KellyN;Andersen,NielsH
β-发夹作为β折叠的简单模型在许多研究小组中得到了普及。本研究的重点是优化β-发夹肽序列，定量残基β倾向，并确定跨链相互作用的能量贡献。研究开始于16个残基的肽（MrH 4 = KKLTVSIXGKKITVSA）。在我们的命名法中，转角基因座残基被指定为T1和T2，其中链位置编号为S±#，这是基于残基在转角位点之前或之后的距离。本研究所探测的位点是S±2和S±4链位点以及T1和T2转角位点。如下所示。
Beta-hairpins have gained popularity in many research groups as simple models for β sheets. The present study focuses on optimizing β-hairpin peptide sequences, quantitating residue β propensities, and determining the energetic contributions from cross-strand interactions. Studies began with the 16-residue peptide (MrH4= KKLTVSIXGKKITVSA). In our nomenclature the turn locus residues are designated as T1 and T2 with strand positions numbered S±# based on how far residues are before or after the turn site. The sites probed in the present study are the S±2 and S±4 strand sites and the T1and T2 turn sites. These are shown below.