摘要: 采用标准化氨基酸疏水性指数将7种Caerins的氨基酸序列转换为28种疏水性(H)或极性(P)的序列，通过二维疏水性–极性(HP)模型分析其全部可能的折叠结构。结果显示Caerins有许多具有相同最小能量的天然形态，这些形态有各种各样对称的折叠结构，而且这些天然形态可以根据标准化的氨基酸疏水性指标进一步从数值上加以区分。这项研究从疏水性–极性角度揭示了Caerin折叠结构的多样性，有助于理解蛋白质的折叠过程，并提示通过工程学方法修改抗菌肽的可能途径。
Abstract:
The amino acid sequences of 7 Caerins were converted into 28 hydrophobic (H) or polar (P) sequences according to the normalized amino acid hydrophobicity index, and all of their possible folding structures were analyzed using 2D hydrophobic-polar (HP) model. The results showed that Caerins have many native states with the same mini- mal energy, which consist of various symmetric folding structures, and that the normalized amino acid hydrophobicity index can help furthermore distinguish native states numerically. The study demonstrates the diversity of Caerin folding structures from hydrophobic-polar (HP) angle, which can shed light on understanding folding process of protein and implying possible ways to modify antimicrobial peptides through engineering.