2-Dimensional HP Folding Structures of Caerin
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.
文章引用: 王何健 , 严少敏 , 吴光 (2012) Caerin的二维HP折叠结构。 计算生物学， 2， 34-41. doi: 10.12677/hjcb.2012.24004
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