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      Estimating the Persistence Length of a Worm-Like Chain Molecule from Force-Extension Measurements

      , , , , ,
      Biophysical Journal
      Elsevier BV

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          Reversible unfolding of individual titin immunoglobulin domains by AFM.

          Single-molecule atomic force microscopy (AFM) was used to investigate the mechanical properties of titin, the giant sarcomeric protein of striated muscle. Individual titin molecules were repeatedly stretched, and the applied force was recorded as a function of the elongation. At large extensions, the restoring force exhibited a sawtoothlike pattern, with a periodicity that varied between 25 and 28 nanometers. Measurements of recombinant titin immunoglobulin segments of two different lengths exhibited the same pattern and allowed attribution of the discontinuities to the unfolding of individual immunoglobulin domains. The forces required to unfold individual domains ranged from 150 to 300 piconewtons and depended on the pulling speed. Upon relaxation, refolding of immunoglobulin domains was observed.
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            Stretching DNA

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              Direct mechanical measurements of the elasticity of single DNA molecules by using magnetic beads

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                Author and article information

                Journal
                Biophysical Journal
                Biophysical Journal
                Elsevier BV
                00063495
                January 1999
                January 1999
                : 76
                : 1
                : 409-413
                Article
                10.1016/S0006-3495(99)77207-3
                9876152
                02d6e8ff-e8b4-4ba4-8c22-6827f5e9c0a6
                © 1999

                http://www.elsevier.com/tdm/userlicense/1.0/

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