Protein adsorption at a gold electrode studied by in situ scanning tunnelling microscopy
The in situ adsorption, under physiological conditions, of azurin molecules at a gold electrode surface has been monitored at the molecular level by scanning tunnelling microscopy. The introduction of free cysteine residues into the surface of the redox protein by structurally conservative mutagenes...
Main Authors: | , , , , , |
---|---|
Formato: | Journal article |
Idioma: | English |
Publicado em: |
1998
|
_version_ | 1826305418738008064 |
---|---|
author | Davis, J Halliwell, C Hill, H Canters, G Amsterdam, v Verbeet, M |
author_facet | Davis, J Halliwell, C Hill, H Canters, G Amsterdam, v Verbeet, M |
author_sort | Davis, J |
collection | OXFORD |
description | The in situ adsorption, under physiological conditions, of azurin molecules at a gold electrode surface has been monitored at the molecular level by scanning tunnelling microscopy. The introduction of free cysteine residues into the surface of the redox protein by structurally conservative mutagenesis allows the immobilisation to be controlled in a manner in which the protein electrochemical activity is retained. |
first_indexed | 2024-03-07T06:32:35Z |
format | Journal article |
id | oxford-uuid:f6848495-73e5-4f3a-8bb7-db5b4d81dc2d |
institution | University of Oxford |
language | English |
last_indexed | 2024-03-07T06:32:35Z |
publishDate | 1998 |
record_format | dspace |
spelling | oxford-uuid:f6848495-73e5-4f3a-8bb7-db5b4d81dc2d2022-03-27T12:35:36ZProtein adsorption at a gold electrode studied by in situ scanning tunnelling microscopyJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:f6848495-73e5-4f3a-8bb7-db5b4d81dc2dEnglishSymplectic Elements at Oxford1998Davis, JHalliwell, CHill, HCanters, GAmsterdam, vVerbeet, MThe in situ adsorption, under physiological conditions, of azurin molecules at a gold electrode surface has been monitored at the molecular level by scanning tunnelling microscopy. The introduction of free cysteine residues into the surface of the redox protein by structurally conservative mutagenesis allows the immobilisation to be controlled in a manner in which the protein electrochemical activity is retained. |
spellingShingle | Davis, J Halliwell, C Hill, H Canters, G Amsterdam, v Verbeet, M Protein adsorption at a gold electrode studied by in situ scanning tunnelling microscopy |
title | Protein adsorption at a gold electrode studied by in situ scanning tunnelling microscopy |
title_full | Protein adsorption at a gold electrode studied by in situ scanning tunnelling microscopy |
title_fullStr | Protein adsorption at a gold electrode studied by in situ scanning tunnelling microscopy |
title_full_unstemmed | Protein adsorption at a gold electrode studied by in situ scanning tunnelling microscopy |
title_short | Protein adsorption at a gold electrode studied by in situ scanning tunnelling microscopy |
title_sort | protein adsorption at a gold electrode studied by in situ scanning tunnelling microscopy |
work_keys_str_mv | AT davisj proteinadsorptionatagoldelectrodestudiedbyinsituscanningtunnellingmicroscopy AT halliwellc proteinadsorptionatagoldelectrodestudiedbyinsituscanningtunnellingmicroscopy AT hillh proteinadsorptionatagoldelectrodestudiedbyinsituscanningtunnellingmicroscopy AT cantersg proteinadsorptionatagoldelectrodestudiedbyinsituscanningtunnellingmicroscopy AT amsterdamv proteinadsorptionatagoldelectrodestudiedbyinsituscanningtunnellingmicroscopy AT verbeetm proteinadsorptionatagoldelectrodestudiedbyinsituscanningtunnellingmicroscopy |