In:
Science, American Association for the Advancement of Science (AAAS), Vol. 301, No. 5631 ( 2003-07-18), p. 367-370
Abstract:
Direct quantification of biomolecular interaction by single-molecule force spectroscopy has evolved into a powerful tool for materials and life sciences. We introduce an approach in which the unbinding forces required to break intermolecular bonds are measured in a differential format by comparison with a known reference bond (here, a short DNAduplex). In addition to a marked increase in sensitivity and force resolution, which enabled us to resolve single–base pair mismatches, this concept allows for highly specific parallel assays. This option was exploited to overcome cross-reactions of antibodies in a protein biochip application.
Type of Medium:
Online Resource
ISSN:
0036-8075
,
1095-9203
DOI:
10.1126/science.1084713
Language:
English
Publisher:
American Association for the Advancement of Science (AAAS)
Publication Date:
2003
detail.hit.zdb_id:
128410-1
detail.hit.zdb_id:
2066996-3
detail.hit.zdb_id:
2060783-0
SSG:
11
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