Surface conformations of an anti-ricin aptamer and its affinity for ricin determined by atomic force microscopy and surface plasmon resonance-Reference-Cited by-同舟云学术

Surface conformations of an anti-ricin aptamer and its affinity for ricin determined by atomic force microscopy and surface plasmon resonance

Published:2015 Issue:1 Volume:17 Page:307-314
ISSN:1463-9076
Container-title:Physical Chemistry Chemical Physics
language:en
Short-container-title:Phys. Chem. Chem. Phys.

Author:

Wang B.¹²³⁴⁵,Lou Z.⁶⁷⁸⁹,Park B.¹⁰¹¹⁴⁵,Kwon Y.¹²¹³¹⁴¹⁵,Zhang H.⁶⁷⁸⁹,Xu B.¹²³⁴⁵

Affiliation:

1. Single Molecule Study Laboratory

2. Faculty of Engineering and Nanoscale Science and Engineering Center

3. University of Georgia

4. Athens

5. USA

6. College of Materials Science and Technology

7. Nanjing University of Aeronautics and Astronautics

8. Nanjing

9. P. R. China

10. USDA-ARS

11. Russell Research Center

12. Avian Disease Division

13. Animal and Plant Quarantine Agency

14. Anyang

15. The Republic of Korea

Abstract

The surface conformations and orientations of an anti-ricin aptamer determine the availability of the specific binding site to ricin molecules and thus determine the binding affinity.

Publisher

Royal Society of Chemistry (RSC)

Subject

Physical and Theoretical Chemistry,General Physics and Astronomy

Link

http://pubs.rsc.org/en/content/articlepdf/2015/CP/C4CP03190C

Reference29 articles.

1. Advances in the study of protein–DNA interaction

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4. Design of PEG-aptamer two piece macromolecules as convenient and integrated sensing platform: Application to the label free detection of small size molecules

5. Following aptamer–ricin specific binding by single molecule recognition and force spectroscopy measurements

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