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

Published online by Cambridge University Press:  21 February 2011

S. M. Amador ,
J. M. Pachence ,
R. Fischetti ,
J. P. McCauley Jr. ,
A. B. Smith III ,
P. L. Dutton  and
J. K. Blasie
S. M. Amador
Affiliation:
Department of Chemistry, Philadelphia PA 19104
J. M. Pachence
Affiliation:
Department of Chemistry, Philadelphia PA 19104
R. Fischetti
Affiliation:
Department of Chemistry, Philadelphia PA 19104
J. P. McCauley Jr.
Affiliation:
Department of Chemistry, Philadelphia PA 19104
A. B. Smith III
Affiliation:
Department of Chemistry, Philadelphia PA 19104
P. L. Dutton
Affiliation:
Department of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia PA 19104
J. K. Blasie
Affiliation:
Department of Chemistry, Philadelphia PA 19104
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Abstract

X-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.

Type
Research Article
Information
MRS Online Proceedings Library (OPL) , Volume 177: Symposium V – Macromolecular Liquids , 1989 , 393
Copyright
Copyright © Materials Research Society 1990

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References

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