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      Mapping flexible protein domains at subnanometer resolution with the atomic force microscope.

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      FEBS letters

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          Abstract

          The mapping of flexible protein domains with the atomic force microscope is reviewed. Examples discussed are the bacteriorhodopsin from Halobacterium salinarum, the head-tail-connector from phage phi29, and the hexagonally packed intermediate layer from Deinococcus radiodurans which all were recorded in physiological buffer solution. All three proteins undergo reversible structural changes that are reflected in standard deviation maps calculated from aligned topographs of individual protein complexes. Depending on the lateral resolution (up to 0.8 nm) flexible surface regions can ultimately be correlated with individual polypeptide loops. In addition, multivariate statistical classification revealed the major conformations of the protein surface.

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          Author and article information

          Affiliations
          [1 ] M.E. Müller-Institute for Microscopy, Biozentrum, University of Basel, Switzerland.
          Journal
          FEBS Lett.
          FEBS letters
          0014-5793
          0014-5793
          Jun 23 1998
          : 430
          : 1-2
          9678604 S0014-5793(98)00623-1

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