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Encapsulating a Single G-Quadruplex Aptamer in a Protein Nanocavity.

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Title: Encapsulating a Single G-Quadruplex Aptamer in a Protein Nanocavity.
Authors: Ji Wook Shim, Li-Qun Gu
Source: Journal of Physical Chemistry B. Jun2008, Vol. 112 Issue 28, p8354-8360. 7p.
Subjects: Biotechnology, Hemostatics, Thrombin, Cations
Abstract: The α-hemolysin (αHL) protein pore has many applications in biotechnology. This article describes a single-molecule manipulation system that utilizes the nanocavity enclosed by this pore to noncovalently encapsulate a guest molecule. The guest is the thrombin-binding aptamer (TBA) that folds into the G-quadruplex in the presence of cations. Trapping the G-quadruplex in the nanocavity resulted in characteristic changes to the pore conductance that revealed important molecular processes, including spontaneous unfolding of the quartet structure and translocation of unfolded DNA in the pore. Through detection with Tag-TBA, we localized the G-quadruplex near the entry of the β-barrel inside the nanocavity, where the molecule vibrates and rotates to different orientations. This guest−nanocavity supramolecular system has potential for helping to understand single-molecule folding and unfolding kinetics. [ABSTRACT FROM AUTHOR]
Copyright of Journal of Physical Chemistry B is the property of American Chemical Society and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
Database: Engineering Source
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Header DbId: egs
DbLabel: Engineering Source
An: 33200502
AccessLevel: 6
PubType: Academic Journal
PubTypeId: academicJournal
PreciseRelevancyScore: 0
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  Data: Encapsulating a Single G-Quadruplex Aptamer in a Protein Nanocavity.
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  Data: <searchLink fieldCode="AR" term="%22Ji+Wook+Shim%22">Ji Wook Shim</searchLink><br /><searchLink fieldCode="AR" term="%22Li-Qun+Gu%22">Li-Qun Gu</searchLink>
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  Data: <searchLink fieldCode="JN" term="%22Journal+of+Physical+Chemistry+B%22">Journal of Physical Chemistry B</searchLink>. Jun2008, Vol. 112 Issue 28, p8354-8360. 7p.
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  Data: <searchLink fieldCode="DE" term="%22Biotechnology%22">Biotechnology</searchLink><br /><searchLink fieldCode="DE" term="%22Hemostatics%22">Hemostatics</searchLink><br /><searchLink fieldCode="DE" term="%22Thrombin%22">Thrombin</searchLink><br /><searchLink fieldCode="DE" term="%22Cations%22">Cations</searchLink>
– Name: Abstract
  Label: Abstract
  Group: Ab
  Data: The α-hemolysin (αHL) protein pore has many applications in biotechnology. This article describes a single-molecule manipulation system that utilizes the nanocavity enclosed by this pore to noncovalently encapsulate a guest molecule. The guest is the thrombin-binding aptamer (TBA) that folds into the G-quadruplex in the presence of cations. Trapping the G-quadruplex in the nanocavity resulted in characteristic changes to the pore conductance that revealed important molecular processes, including spontaneous unfolding of the quartet structure and translocation of unfolded DNA in the pore. Through detection with Tag-TBA, we localized the G-quadruplex near the entry of the β-barrel inside the nanocavity, where the molecule vibrates and rotates to different orientations. This guest−nanocavity supramolecular system has potential for helping to understand single-molecule folding and unfolding kinetics. [ABSTRACT FROM AUTHOR]
– Name: AbstractSuppliedCopyright
  Label:
  Group: Ab
  Data: <i>Copyright of Journal of Physical Chemistry B is the property of American Chemical Society and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
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RecordInfo BibRecord:
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    Identifiers:
      – Type: doi
        Value: 10.1021/jp0775911
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      – Code: eng
        Text: English
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      Pagination:
        PageCount: 7
        StartPage: 8354
    Subjects:
      – SubjectFull: Biotechnology
        Type: general
      – SubjectFull: Hemostatics
        Type: general
      – SubjectFull: Thrombin
        Type: general
      – SubjectFull: Cations
        Type: general
    Titles:
      – TitleFull: Encapsulating a Single G-Quadruplex Aptamer in a Protein Nanocavity.
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            NameFull: Ji Wook Shim
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            NameFull: Li-Qun Gu
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              Text: Jun2008
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              Y: 2008
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              Value: 112
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              Value: 28
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            – TitleFull: Journal of Physical Chemistry B
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