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  • Title: Force spectroscopy of barnase-barstar single molecule interaction.
    Author: Sekatskii SK, Favre M, Dietler G, Mikhailov AG, Klinov DV, Lukash SV, Deyev SM.
    Journal: J Mol Recognit; 2010; 23(6):583-8. PubMed ID: 21038358.
    Abstract:
    Results of the single molecule force spectroscopy study of specific interactions between ribonuclease barnase and its inhibitor barstar are presented. Experimental data obtained for the force loading rate ranging 2-70 nN/s are well approximated by a single straight line, from which the dissociation barrier of the width of 0.12 nm and height of 0.75-0.85 × 10(-19)J can be inferred. The measured value of specific interaction does not depend on the NaCl concentration. This apparently contradicts the well-known dependence of the binding energy of this pair on the salt concentration, but such a "contradiction" is explained by the insensitivity of the force spectroscopy data to the relatively long-range electrostatic interaction. The latter essentially contributes to the value of barnase-barstar binding energy revealed by biochemical measurements, and it is exactly this electrostatic interaction which is influenced by the salt concentration.
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