journal article·2014-07

An Entropic Force Microscope Enables Nano‐Scale Conformational Probing of Biomolecules

Nan Shi, Victor M. Ugaz

Small· Volume 10· Issue 13
Publisher page

Abstract

Inherently disordered dynamics governing macromolecular transport under nanoconfined surroundings can paradoxically be precisely controlled. This capability lays a foundation for a sensitive probe of nanoscale molecular conformation, revealing previously unseen details about DNA-protein binding interactions at size scales below the limits of most conventional techniques. As a service to our authors and readers, this journal provides supporting information supplied by the authors. Such materials are peer reviewed and may be re-organized for online delivery, but are not copy-edited or typeset. Technical support issues arising from supporting information (other than missing files) should be addressed to the authors. Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.
Source: openalex_inverted_index · Quality: baseline

Research context

OpenAlex topics: Force Microscopy Techniques and Applications · Nanopore and Nanochannel Transport Studies · Advanced Electron Microscopy Techniques and Applications

SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.

Affiliations

Artie McFerrin Department of Chemical Engineering Texas A&M University 3122 TAMU College Station Texas 77843 USA

References (34)

Show source-provided references
1. 10.1021/ac202358t10.1021/ac202358t ↗
2. 10.1126/science.119338310.1126/science.1193383 ↗
3. 10.1103/PhysRevLett.97.01810310.1103/PhysRevLett.97.018103 ↗
4. 10.1103/RevModPhys.82.290310.1103/RevModPhys.82.2903 ↗
5. 10.1023/A:101605671576210.1023/A:1016056715762 ↗
6. 10.1002/1522-2683(200012)21:18<3873::AID-ELPS3873>3.0.CO;2-810.1002/1522-2683(200012)21:18<3873::AID-ELPS3873>3.0.CO;2-8 ↗
7. 10.1016/S0031-8914(40)90098-210.1016/S0031-8914(40)90098-2 ↗
8. 10.1103/RevModPhys.70.22310.1103/RevModPhys.70.223 ↗
9. 10.1016/j.plrev.2010.06.00110.1016/j.plrev.2010.06.001 ↗
10. 10.1016/S0006-3495(02)75672-510.1016/S0006-3495(02)75672-5 ↗
11. 10.1002/bip.2112310.1002/bip.21123 ↗
12. 10.1088/0957-4484/16/10/05510.1088/0957-4484/16/10/055 ↗
13. 10.1016/j.jmb.2008.01.06710.1016/j.jmb.2008.01.067 ↗
14. 10.1093/nar/gkp31710.1093/nar/gkp317 ↗
15. 10.1021/nl903631m10.1021/nl903631m ↗
16. 10.1021/nl300282710.1021/nl3002827 ↗
17. 10.1021/nl803189k10.1021/nl803189k ↗
18. 10.1021/nl901691v10.1021/nl901691v ↗
19. 10.1002/adma.20080130310.1002/adma.200801303 ↗
20. 10.1016/S0006-3495(03)74624-410.1016/S0006-3495(03)74624-4 ↗
21. 10.1529/biophysj.103.03629310.1529/biophysj.103.036293 ↗
22. 10.1093/nar/gkq43410.1093/nar/gkq434 ↗
23. 10.1103/PhysRevLett.105.10810110.1103/PhysRevLett.105.108101 ↗
24. 10.1103/RevModPhys.72.81310.1103/RevModPhys.72.813 ↗
25. 10.1063/1.44521010.1063/1.445210 ↗
26. 10.1124/pr.56.2.610.1124/pr.56.2.6 ↗
27. 10.1073/pnas.95.20.1156110.1073/pnas.95.20.11561 ↗
28. 10.1093/nar/28.4.101910.1093/nar/28.4.1019 ↗
29. 10.1126/science.271.5250.79210.1126/science.271.5250.792 ↗
30. 10.1073/pnas.73.3.80410.1073/pnas.73.3.804 ↗
31. 10.1002/1438-5171(200206)3:2/3<97::AID-SIMO97>3.0.CO;2-S10.1002/1438-5171(200206)3:2/3<97::AID-SIMO97>3.0.CO;2-S ↗
32. 10.1016/j.copbio.2007.09.00610.1016/j.copbio.2007.09.006 ↗
33. 10.1146/annurev-bioeng-071811-15011810.1146/annurev-bioeng-071811-150118 ↗
34. 10.1039/b811033f10.1039/b811033f ↗