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The Orientations of Large Aspect-Ratio Coiled-Coil Proteins Attached to Gold Nanostructures.

Authors :
Chang JB
Kim YH
Thompson E
No YH
Kim NH
Arrieta J
Manfrinato VR
Keating AE
Berggren KK
Source :
Small (Weinheim an der Bergstrasse, Germany) [Small] 2016 Mar; Vol. 12 (11), pp. 1498-505. Date of Electronic Publication: 2016 Jan 21.
Publication Year :
2016

Abstract

Methods for patterning biomolecules on a substrate at the single molecule level have been studied as a route to sensors with single-molecular sensitivity or as a way to probe biological phenomena at the single-molecule level. However, the arrangement and orientation of single biomolecules on substrates has been less investigated. Here, the arrangement and orientation of two rod-like coiled-coil proteins, cortexillin and tropomyosin, around patterned gold nanostructures is examined. The high aspect ratio of the coiled coils makes it possible to study their orientations and to pursue a strategy of protein orientation via two-point attachment. The proteins are anchored to the surfaces using thiol groups, and the number of cysteine residues in tropomyosin is varied to test how this variation affects the structure and arrangement of the surface-attached proteins. Molecular dynamics studies are used to interpret the observed positional distributions. Based on initial studies of protein attachment to gold post structures, two 31-nm-long tropomyosin molecules are aligned between the two sidewalls of a trench with a width of 68 nm. Because the approach presented in this study uses one of twenty natural amino acids, this method provides a convenient way to pattern biomolecules on substrates using standard chemistry.<br /> (© 2016 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.)

Details

Language :
English
ISSN :
1613-6829
Volume :
12
Issue :
11
Database :
MEDLINE
Journal :
Small (Weinheim an der Bergstrasse, Germany)
Publication Type :
Academic Journal
Accession number :
26799936
Full Text :
https://doi.org/10.1002/smll.201502419