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      Gold nanoparticle-cytochrome C complexes: the effect of nanoparticle ligand charge on protein structure.

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          Abstract

          We report the effect of nanoparticle ligand charge on the structure of a covalently, site-specifically linked protein. Au nanoparticles with positive, negative, and neutral ligands were appended to a specific cysteine, C102, of Saccharomyces cerevisiae cytochrome c. Conjugates were purified by HPLC or gel electrophoresis. Circular dichroism spectroscopy shows that changing the nanoparticle ligand dramatically influences the attached cytochrome c structure. The protein retains its structure with neutral ligands but denatures in the presence of charged species. This is rationalized by the electrostatic interaction of amino acids in the local vicinity of C102 with the endgroups of the ligand.

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          Author and article information

          Journal
          Langmuir
          Langmuir : the ACS journal of surfaces and colloids
          American Chemical Society (ACS)
          0743-7463
          0743-7463
          Dec 20 2005
          : 21
          : 26
          Affiliations
          [1 ] Department of Mechanical Engineering and the Biological Engineering Division, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA.
          Article
          10.1021/la052102e
          16342975
          bd9c74cb-3b60-4139-b264-dd57646eb027
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