期刊
NATURE NANOTECHNOLOGY
卷 9, 期 10, 页码 835-840出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/NNANO.2014.193
关键词
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资金
- Japan Society for the Promotion of Science (JSPS) through its Program for World-Leading Innovative R&D on Science and Technology
- KAKENHI [26220603]
- Grants-in-Aid for Scientific Research [24681032, 26220603] Funding Source: KAKEN
Post-translational modifications alter the properties of proteins through the cleavage of peptide bonds or the addition of a modifying group to one or more amino acids(1-7). These modifications allow proteins to perform their primary biological functions(8-11), but single-protein studies of post-translational modifications have been hindered by a lack of suitable analysis methods(12-16). Here, we show that single amino acids can be identified using electron tunnelling currents measured as the individual molecules pass through a nanoscale gap between electrodes. We identify 12 different amino acids and the post-translational modification phosphotyrosine, which is involved in the process that switches enzymes on and off(17-20). Furthermore, we show that the conductance measurements can be used to partially sequence peptides of an epidermal growth factor receptor substrate, and can discriminate a peptide from its phosphorylated variant.
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