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231223s2008 xx ||||| 00| ||eng c |
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|a pubmed24n0583.xml
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|a (DE-627)NLM175000018
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|a (NLM)18001070
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|a DE-627
|b ger
|c DE-627
|e rakwb
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| 041 |
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|a eng
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| 100 |
1 |
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|a Tang, Jilin
|e verfasserin
|4 aut
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| 245 |
1 |
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|a High-affinity tags fused to s-layer proteins probed by atomic force microscopy
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|c 2008
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|a Text
|b txt
|2 rdacontent
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|a ohne Hilfsmittel zu benutzen
|b n
|2 rdamedia
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|a Band
|b nc
|2 rdacarrier
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| 500 |
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|a Date Completed 07.05.2008
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|a Date Revised 01.12.2018
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a Two-dimensional, crystalline bacterial cell surface layers, termed S-layers, are one of the most commonly observed cell surface structures of prokaryotic organisms. In the present study, genetically modified S-layer protein SbpA of Bacillus sphaericus CCM 2177 carrying the short affinity peptide Strep-tag I or Strep-tag II at the C terminus was used to generate a 2D crystalline monomolecular protein lattice on a silicon surface. Because of the genetic modification, the 2D crystals were addressable via Strep-tag through streptavidin molecules. Atomic force microscopy (AFM) was used to investigate the topography of the single-molecules array and the functionality of the fused Strep-tags. In high-resolution imaging under near-physiological conditions, structural details such as protein alignment and spacing were resolved. By applying molecular recognition force microscopy, the Strep-tag moieties were proven to be fully functional and accessible. For this purpose, streptavidin molecules were tethered to AFM tips via approximately 8-nm-long flexible polyethylene glycol (PEG) linkers. These functionalized tips showed specific interactions with 2D protein crystals containing either the Strep-tag I or Strep-tag II, with similar energetic and kinetic behavior in both cases
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Research Support, U.S. Gov't, Non-P.H.S.
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| 650 |
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|a Membrane Glycoproteins
|2 NLM
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|a S-layer proteins
|2 NLM
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|a Polyethylene Glycols
|2 NLM
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|a 3WJQ0SDW1A
|2 NLM
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| 650 |
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|a Streptavidin
|2 NLM
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| 650 |
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|a 9013-20-1
|2 NLM
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| 650 |
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|a Silicon
|2 NLM
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| 650 |
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|a Z4152N8IUI
|2 NLM
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| 700 |
1 |
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|a Ebner, Andreas
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Ilk, Nicola
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Lichtblau, Helga
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Huber, Carina
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Zhu, Rong
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Pum, Dietmar
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Leitner, Micheal
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Pastushenko, Vassili
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Gruber, Hermann J
|e verfasserin
|4 aut
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| 700 |
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|a Sleytr, Uwe B
|e verfasserin
|4 aut
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| 700 |
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|a Hinterdorfer, Peter
|e verfasserin
|4 aut
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| 773 |
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|i Enthalten in
|t Langmuir : the ACS journal of surfaces and colloids
|d 1992
|g 24(2008), 4 vom: 19. Feb., Seite 1324-9
|w (DE-627)NLM098181009
|x 1520-5827
|7 nnns
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| 773 |
1 |
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|g volume:24
|g year:2008
|g number:4
|g day:19
|g month:02
|g pages:1324-9
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