Unfolding stabilities of two structurally similar proteins as probed by temperature-induced and force-induced molecular dynamics simulations.

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  • Author(s): Gorai B;Gorai B; Prabhavadhni A; Sivaraman T
  • Source:
    Journal of biomolecular structure & dynamics [J Biomol Struct Dyn] 2015 Sep; Vol. 33 (9), pp. 2037-47. Date of Electronic Publication: 2014 Dec 12.
  • Publication Type:
    Journal Article; Research Support, Non-U.S. Gov't
  • Language:
    English
  • Additional Information
    • Source:
      Publisher: Taylor & Francis Country of Publication: England NLM ID: 8404176 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1538-0254 (Electronic) Linking ISSN: 07391102 NLM ISO Abbreviation: J Biomol Struct Dyn Subsets: MEDLINE
    • Publication Information:
      Publication: June 2012- : Oxon, UK : Taylor & Francis
      Original Publication: Guilderland, NY : Adenine Press, [c1983-
    • Subject Terms:
      Molecular Dynamics Simulation* ; Protein Conformation* ; Protein Unfolding*; Proteins/*chemistry; Protein Folding ; Temperature ; Thermodynamics
    • Abstract:
      Unfolding stabilities of two homologous proteins, cardiotoxin III and short-neurotoxin (SNTX) belonging to three-finger toxin (TFT) superfamily, have been probed by means of molecular dynamics (MD) simulations. Combined analysis of data obtained from steered MD and all-atom MD simulations at various temperatures in near physiological conditions on the proteins suggested that overall structural stabilities of the two proteins were different from each other and the MD results are consistent with experimental data of the proteins reported in the literature. Rationalization for the differential structural stabilities of the structurally similar proteins has been chiefly attributed to the differences in the structural contacts between C- and N-termini regions in their three-dimensional structures, and the findings endorse the 'CN network' hypothesis proposed to qualitatively analyse the thermodynamic stabilities of proteins belonging to TFT superfamily of snake venoms. Moreover, the 'CN network' hypothesis has been revisited and the present study suggested that 'CN network' should be accounted in terms of 'structural contacts' and 'structural strengths' in order to precisely describe order of structural stabilities of TFTs.
    • Contributed Indexing:
      Keywords: CN network; mechanical stability; molecular dynamics; protein folds; temperature-induced unfolding
    • Accession Number:
      0 (Proteins)
    • Publication Date:
      Date Created: 20141112 Date Completed: 20160419 Latest Revision: 20150716
    • Publication Date:
      20221213
    • Accession Number:
      10.1080/07391102.2014.986668
    • Accession Number:
      25387083