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Article citations


Phillips, J.C., Braun, R., Wang, W., Gumbart, J., Tajkhorshid, E., Villa, E., Chipot, C., Skeel, R.D., Kalé, L. and Schulten, K. (2005) Scalable Molecular Dynamics with NAMD. Journal of Computational Chemistry, 26, 1781-1802.

has been cited by the following article:

  • TITLE: Spontaneous Unfolding and Refolding of Plantaricin α-Helix in Molecular Dynamics Simulation

    AUTHORS: Shaomin Yan, Guang Wu

    KEYWORDS: Alpha-Helix, Antimicrobial Peptides, Protein Folding, Plantaricin A

    JOURNAL NAME: Computational Molecular Bioscience, Vol.9 No.1, March 28, 2019

    ABSTRACT: Antimicrobial peptides are promising therapeutic agents in view of increasing resistance to conventional antibiotics. Antimicrobial peptides usually fold in α-helical, β-sheet, and extended/random-coil structures. The α-helical antimicrobial peptides are often unstructured in aqueous solution but become structured on bacterial membrane. The α-helical structure allows the partitioning into bacterial membrane. Therefore it is important to understand the mechanism of unfolding and refolding of α-helical structure in antimicrobial peptides. It is not very easy to obverse and study the process of unfolding and refolding of α-helical antimicrobial peptides because of their rapidity. Therefore, molecular simulation provides a way to observe and explain this phenomenon. Plantaricin A is a 26 amino-acid antimicrobial pheromone peptide and can spontaneously unfold and refold under physiological condition. This study demonstrated the unfolding and refolding of plantaricin A by means of molecular simulation, and its mechanism was discussed with its implication to the Levinthal paradox.