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231223s2004 xx ||||| 00| ||eng c |
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|a pubmed24n0500.xml
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|a (DE-627)NLM150026056
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|a (NLM)15323527
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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| 100 |
1 |
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|a Stevens, Molly M
|e verfasserin
|4 aut
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| 245 |
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|a pH-dependent behavior of surface-immobilized artificial leucine zipper proteins
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| 264 |
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1 |
|c 2004
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| 336 |
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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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| 338 |
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|a Band
|b nc
|2 rdacarrier
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| 500 |
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|a Date Completed 10.03.2006
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|a Date Revised 15.11.2006
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|a published: Print
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|a Citation Status MEDLINE
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| 520 |
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|a The coiled-coil protein motif occurs in over 200 proteins and has generated interest for a range of applications requiring surface immobilization of the constituent peptides. This paper describes an investigation of the environment-responsive behavior of a monolayer of surface-immobilized artificial proteins, which are known to assemble to form coiled-coil structures in bulk solution. An extended version of the quartz crystal microbalance (QCM-D) and surface plasmon resonance (SPR) are independently employed to characterize the adsorption of the proteins to a gold surface. The data suggest that the molecules arrange in a closely packed layer orientated perpendicular to the surface. QCM-D measurements are also employed to measure pH-induced changes in the resonant frequency (f) and the energy dissipation factor (D) of a gold-coated quartz crystal functionalized with the formed monolayer. Exposure of the protein monolayer to a pH 4.5 solution results in a shift of 43 Hz in f and a shift of -0.7 x 10(-6) in D as compared to pH 7.4. In contrast, increasing the pH to 11.2, results in f and D shifts of -17 Hz and 0.6 x 10(-6), respectively. The magnitude of the observed shifts suggests that the proteins form a rigid layer at low pH that can be hydrated to a fluid layer as the pH is increased. These observations correlate with spectroscopic changes that indicate a reduction in the helical content of the protein in bulk solutions of high pH
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| 650 |
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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| 650 |
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|a Research Support, U.S. Gov't, Non-P.H.S.
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| 650 |
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7 |
|a Coated Materials, Biocompatible
|2 NLM
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| 650 |
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|a Membrane Proteins
|2 NLM
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| 650 |
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|a Quartz
|2 NLM
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| 650 |
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|a 14808-60-7
|2 NLM
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| 650 |
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|a Gold
|2 NLM
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| 650 |
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|a 7440-57-5
|2 NLM
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| 700 |
1 |
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|a Allen, Stephanie
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Sakata, Jill K
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Davies, Martyn C
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Roberts, Clive J
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Tendler, Saul J B
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Tirrell, David A
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Williams, Philip M
|e verfasserin
|4 aut
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| 773 |
0 |
8 |
|i Enthalten in
|t Langmuir : the ACS journal of surfaces and colloids
|d 1992
|g 20(2004), 18 vom: 31. Aug., Seite 7747-52
|w (DE-627)NLM098181009
|x 1520-5827
|7 nnns
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| 773 |
1 |
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|g volume:20
|g year:2004
|g number:18
|g day:31
|g month:08
|g pages:7747-52
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|a GBV_USEFLAG_A
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|a GBV_NLM
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|a GBV_ILN_350
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|a GBV_ILN_721
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|a AR
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|d 20
|j 2004
|e 18
|b 31
|c 08
|h 7747-52
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