A scanning tunnelling microscopy study of Clostridium pasteurianum rubredoxin.
Scanning tunnelling microscopy (STM), which can provide 'direct' and 'non-averaged' information on molecular structure in three dimensions, has been used to achieve sub-molecular resolution in a 'single molecule' of rubredoxin, an important iron-sulphur protein, at the...
| Main Authors: | , , , , |
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| Format: | Journal article |
| Language: | English |
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2000
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| _version_ | 1826264575481217024 |
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| author | Mukhopadhyay, R Davis, J Kyritsis, P Hill, H Meyer, J |
| author_facet | Mukhopadhyay, R Davis, J Kyritsis, P Hill, H Meyer, J |
| author_sort | Mukhopadhyay, R |
| collection | OXFORD |
| description | Scanning tunnelling microscopy (STM), which can provide 'direct' and 'non-averaged' information on molecular structure in three dimensions, has been used to achieve sub-molecular resolution in a 'single molecule' of rubredoxin, an important iron-sulphur protein, at the gold (111)/water interface. The metal-ligand site [Fe(III)-Cys4] appears distinct because of an enhancement of the tunnelling current over this region compared to the surrounding protein structure. |
| first_indexed | 2024-03-06T20:10:02Z |
| format | Journal article |
| id | oxford-uuid:2a3dcbd3-1bd9-424c-9d8f-8338af49ee65 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T20:10:02Z |
| publishDate | 2000 |
| record_format | dspace |
| spelling | oxford-uuid:2a3dcbd3-1bd9-424c-9d8f-8338af49ee652022-03-26T12:23:54ZA scanning tunnelling microscopy study of Clostridium pasteurianum rubredoxin.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:2a3dcbd3-1bd9-424c-9d8f-8338af49ee65EnglishSymplectic Elements at Oxford2000Mukhopadhyay, RDavis, JKyritsis, PHill, HMeyer, JScanning tunnelling microscopy (STM), which can provide 'direct' and 'non-averaged' information on molecular structure in three dimensions, has been used to achieve sub-molecular resolution in a 'single molecule' of rubredoxin, an important iron-sulphur protein, at the gold (111)/water interface. The metal-ligand site [Fe(III)-Cys4] appears distinct because of an enhancement of the tunnelling current over this region compared to the surrounding protein structure. |
| spellingShingle | Mukhopadhyay, R Davis, J Kyritsis, P Hill, H Meyer, J A scanning tunnelling microscopy study of Clostridium pasteurianum rubredoxin. |
| title | A scanning tunnelling microscopy study of Clostridium pasteurianum rubredoxin. |
| title_full | A scanning tunnelling microscopy study of Clostridium pasteurianum rubredoxin. |
| title_fullStr | A scanning tunnelling microscopy study of Clostridium pasteurianum rubredoxin. |
| title_full_unstemmed | A scanning tunnelling microscopy study of Clostridium pasteurianum rubredoxin. |
| title_short | A scanning tunnelling microscopy study of Clostridium pasteurianum rubredoxin. |
| title_sort | scanning tunnelling microscopy study of clostridium pasteurianum rubredoxin |
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