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Search for "amino acid" in Full Text gives 77 result(s) in Beilstein Journal of Nanotechnology.

Detection of interaction between biomineralising proteins and calcium carbonate microcrystals

  • Hanna Rademaker and
  • Malte Launspach

Beilstein J. Nanotechnol. 2011, 2, 222–227, doi:10.3762/bjnano.2.26

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  • . These two protein bands (one at approx. 19 kDa and the other at about 25 kDa) belong to the protein perlucin [10]. The corresponding fractions of purified protein showing these two bands on SDS-PAGEs had been subjected to N-terminal amino acid sequence analysis [11] in several different experiments
  • of perlucin has saccharide oligomers bound to these sites. In MALDI-MS (matrix-assisted laser desorption/ionization mass spectroscopy) of perlucin [10] variable molecular weights of perlucin are detectable, which can be related to a 10 amino acid repeat at the C-terminus being present in various
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Published 27 Apr 2011

Electrochemical behavior of dye-linked L-proline dehydrogenase on glassy carbon electrodes modified by multi-walled carbon nanotubes

  • Haitao Zheng,
  • Leyi Lin,
  • Yosuke Okezaki,
  • Ryushi Kawakami,
  • Haruhiko Sakuraba,
  • Toshihisa Ohshima,
  • Keiichi Takagi and
  • Shin-ichiro Suye

Beilstein J. Nanotechnol. 2010, 1, 135–141, doi:10.3762/bjnano.1.16

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  • typical Michaelis–Menten catalytic response with lower apparent constant. Keywords: dye-linked L-proline dehydrogenase; electrocatalysis; electron transfer; multi-walled carbon nanotube; Introduction As an essential amino acid for the proper functioning of tendons and joints in the human body, the quick
  • for the detection of various types of chemical or biochemical substances [18][19][20][21][22][23]. Some amino acid biosensors have already been reported based on CNTs-modified electrodes [24][25][26][27]. In our previous work, the recombinant thermostable dye-linked L-proline dehydrogenase (L-proDH
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Published 14 Dec 2010
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