Nucleobase recognition in ssDNA at the central constriction of the alpha-hemolysin pore.
Nanopores are under investigation for single-molecule DNA sequencing. The alpha-hemolysin (alphaHL) protein nanopore contains three recognition points capable of nucleobase discrimination in individual immobilized ssDNA molecules. We have modified the recognition point R(1) by extensive mutagenesis...
| 主要な著者: | , , , , , |
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| フォーマット: | Journal article |
| 言語: | English |
| 出版事項: |
2010
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| _version_ | 1826268881588584448 |
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| author | Stoddart, D Heron, A Klingelhoefer, J Mikhailova, E Maglia, G Bayley, H |
| author_facet | Stoddart, D Heron, A Klingelhoefer, J Mikhailova, E Maglia, G Bayley, H |
| author_sort | Stoddart, D |
| collection | OXFORD |
| description | Nanopores are under investigation for single-molecule DNA sequencing. The alpha-hemolysin (alphaHL) protein nanopore contains three recognition points capable of nucleobase discrimination in individual immobilized ssDNA molecules. We have modified the recognition point R(1) by extensive mutagenesis of residue 113. Amino acids that provide an energy barrier to ion flow (e.g., bulky or hydrophobic residues) strengthen base identification, while amino acids that lower the barrier weaken it. Amino acids with related side chains produce similar patterns of nucleobase recognition providing a rationale for the redesign of recognition points. |
| first_indexed | 2024-03-06T21:16:22Z |
| format | Journal article |
| id | oxford-uuid:3fee24f7-0c7e-4df8-841b-80f7a517514a |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T21:16:22Z |
| publishDate | 2010 |
| record_format | dspace |
| spelling | oxford-uuid:3fee24f7-0c7e-4df8-841b-80f7a517514a2022-03-26T14:34:56ZNucleobase recognition in ssDNA at the central constriction of the alpha-hemolysin pore.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:3fee24f7-0c7e-4df8-841b-80f7a517514aEnglishSymplectic Elements at Oxford2010Stoddart, DHeron, AKlingelhoefer, JMikhailova, EMaglia, GBayley, HNanopores are under investigation for single-molecule DNA sequencing. The alpha-hemolysin (alphaHL) protein nanopore contains three recognition points capable of nucleobase discrimination in individual immobilized ssDNA molecules. We have modified the recognition point R(1) by extensive mutagenesis of residue 113. Amino acids that provide an energy barrier to ion flow (e.g., bulky or hydrophobic residues) strengthen base identification, while amino acids that lower the barrier weaken it. Amino acids with related side chains produce similar patterns of nucleobase recognition providing a rationale for the redesign of recognition points. |
| spellingShingle | Stoddart, D Heron, A Klingelhoefer, J Mikhailova, E Maglia, G Bayley, H Nucleobase recognition in ssDNA at the central constriction of the alpha-hemolysin pore. |
| title | Nucleobase recognition in ssDNA at the central constriction of the alpha-hemolysin pore. |
| title_full | Nucleobase recognition in ssDNA at the central constriction of the alpha-hemolysin pore. |
| title_fullStr | Nucleobase recognition in ssDNA at the central constriction of the alpha-hemolysin pore. |
| title_full_unstemmed | Nucleobase recognition in ssDNA at the central constriction of the alpha-hemolysin pore. |
| title_short | Nucleobase recognition in ssDNA at the central constriction of the alpha-hemolysin pore. |
| title_sort | nucleobase recognition in ssdna at the central constriction of the alpha hemolysin pore |
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