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Volumn 301, Issue 5631, 2003, Pages 367-370

DNA: A programmable force sensor

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBODIES; BIOSENSORS; CHEMICAL BONDS;

EID: 0038638476     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.1084713     Document Type: Article
Times cited : (156)

References (51)
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    • note
    • In conventional force spectroscopy, molecular forces are measured as displacements against spring constants or trap slopes. Because the nature of intra- and intermolecular forces is fundamentally different from metal or silicon springs (or from optical or magnetic traps), all kinds of fluctuations or drifts, such as temperature and pH, will alter the measured signal. In the differential molecular format, each cancels out the effects of the other.
  • 24
    • 0038450976 scopus 로고    scopus 로고
    • note
    • B is Boltzmann's constant, T is temperature, and l is the characteristic width of the binding potential. Consequently, the window of possible reference forces is broadened by approximately the same amount (49, 50).
  • 25
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    • note
    • This is true as long as the lateral density is kept below the fluorescence resonance energy transfer limit.
  • 29
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    • note
    • Different optical and chemical properties, as well as differences in coupling efficiencies to the two surfaces, are compensated in this way.
  • 33
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    • note
    • The discrimination between mismatch and perfect match could clearly be improved by decreasing the salt concentration or increasing the temperature and making use of both spontaneous and force-induced strand separation. However, in this study, we focused on forced unbinding events.
  • 34
    • 10244219858 scopus 로고    scopus 로고
    • M. Chee et al., Science 274, 610 (1996).
    • (1996) Science , vol.274 , pp. 610
    • Chee, M.1
  • 39
    • 0038788592 scopus 로고    scopus 로고
    • note
    • BT/l can be resolved.
  • 44
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    • A. Abbott, Nature 415, 112 (2002).
    • (2002) Nature , vol.415 , pp. 112
    • Abbott, A.1
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    • data not shown
    • C. Abrecht et al., data not shown.
    • Abrecht, C.1
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    • G. MacBeath, Nature Genet. 32 (suppl. 2), 526 (2002).
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    • MacBeath, G.1
  • 51
    • 0038788598 scopus 로고    scopus 로고
    • note
    • We thank M. Rief for kindly providing the total internal reflection flourescence (TIRF) data showing single-molecule fluorescence, M. Benoit for technical support, F. Oesterhelt, C. Duschl, and D. Mendik for helpful discussions. Supported by the Nanobiotechnology and Proteomics program of the Bundesministerium for Bildung and Forschung (grants 13N8141 and O312821A) and the Bayerische Forschungsstiftung.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.