X-Ray Diffraction Studies of Protein Monolayers Bound to Self-Assembled Monolayers

1989 ◽  
Vol 177 ◽  
Author(s):  
S. M. Amador ◽  
J. M. Pachence ◽  
R. Fischetti ◽  
J. P. McCauley ◽  
A. B. Smith ◽  
...  

ABSTRACTX-ray interferometry was used to study monolayers of the protein yeast cytochrome c and a bimolecular cytochrome c/photosynthetic reaction center complex bound to self-assembled monolayers of 11-trichlorosilylundecyl thiol on inorganic substrates. Optical absorption spectroscopy and dissociation experiments show that the cytochrome c monolayer is covalently attached to the self-assembled monolayer via a disulfide bond and they are consistent with the cytochrome c and its bimolecular reaction center complex forming a close-packed array on the surface of the solid substrate. By sequentially forming these bio-organic monolayers on synthetic inorganic multilayers (“quantum wells”), we were able to determine the electron density profile of the protein layers to ∼13 Å resolution using x-ray interferometry and refinement techniques.

2012 ◽  
Vol 3 ◽  
pp. 12-24 ◽  
Author(s):  
Hicham Hamoudi ◽  
Ping Kao ◽  
Alexei Nefedov ◽  
David L Allara ◽  
Michael Zharnikov

Self-assembled monolayers (SAMs) of nitrile-substituted oligo(phenylene ethynylene) thiols (NC-OPEn) with a variable chain length n (n ranging from one to three structural units) on Au(111) were studied by synchrotron-based high-resolution X-ray photoelectron spectroscopy and near-edge absorption fine-structure spectroscopy. The experimental data suggest that the NC-OPEn molecules form well-defined SAMs on Au(111), with all the molecules bound to the substrate through the gold–thiolate anchor and the nitrile tail groups located at the SAM–ambient interface. The packing density in these SAMs was found to be close to that of alkanethiolate monolayers on Au(111), independent of the chain length. Similar behavior was found for the molecular inclination, with an average tilt angle of ~33–36° for all the target systems. In contrast, the average twist of the OPEn backbone (planar conformation) was found to depend on the molecular length, being close to 45° for the films comprising the short OPE chains and ~53.5° for the long chains. Analysis of the data suggests that the attachment of the nitrile moiety, which served as a spectroscopic marker group, to the OPEn backbone did not significantly affect the molecular orientation in the SAMs.


Langmuir ◽  
2004 ◽  
Vol 20 (16) ◽  
pp. 6964-6964 ◽  
Author(s):  
Young-Hye La ◽  
Yu Jin Jung ◽  
Hyun Ju Kim ◽  
Tai-Hee Kang ◽  
Kyuwook Ihm ◽  
...  

Langmuir ◽  
1997 ◽  
Vol 13 (7) ◽  
pp. 1881-1883 ◽  
Author(s):  
Stanislaw Petrash ◽  
Nina B. Sheller ◽  
William Dando ◽  
Mark D. Foster

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