Chemical Laboratory, Central Leather Research Institute, (Council of Scientific and Industrial Research, India), Adyar, Chennai 600020, India.
J Biomed Nanotechnol. 2011 Feb;7(1):87-8. doi: 10.1166/jbn.2011.1215.
In this study a thorough investigation on the changes in the conformation of the alpha-helical peptide on interaction with CNTs has been attempted using classical molecular dynamics simulation. The primary objective of this investigation is to understand the changes in the conformation of the longer alpha-helical peptides on interaction with CNTs. The results show that the helix propensity of the amino acids present in the sequence has a direct influence on the mode of so that the regions which are composed of the amino acids having low helix propensity would undergo unfolding in the presence of CNT.
在这项研究中，我们尝试使用经典分子动力学模拟，深入研究了α-螺旋肽与 CNT 相互作用时构象的变化。这项研究的主要目的是了解较长的α-螺旋肽与 CNT 相互作用时构象的变化。结果表明，序列中氨基酸的螺旋倾向对其方式有直接影响，因此，由螺旋倾向较低的氨基酸组成的区域在存在 CNT 时会发生展开。
