| Helix-coil kinetics of individual polyadenylic acid molecules in a protein channel. | |
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MedLine Citation:
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PMID: 20482020 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Helix-coil transition kinetics of polyadenylic acid [poly(A)] inside a small protein channel is investigated for the first time, at the single molecule level. The confinement of a RNA molecule inside the channel slows its kinetics by nearly 3 orders of magnitude as compared to bulk measurements of free poly(A). These findings are related to the interaction energy of the RNA structure with the interior of the pore, explained by a simple two-state model. These results shed light on the way intermolecular interactions alter nucleic acid kinetics. |
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Authors:
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Jianxun Lin; Anatoly Kolomeisky; Amit Meller |
Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S. Date: 2010-04-15 |
Journal Detail:
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Title: Physical review letters Volume: 104 ISSN: 1079-7114 ISO Abbreviation: Phys. Rev. Lett. Publication Date: 2010 Apr |
Date Detail:
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Created Date: 2010-05-20 Completed Date: 2010-08-11 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 0401141 Medline TA: Phys Rev Lett Country: United States |
Other Details:
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Languages: eng Pagination: 158101 Citation Subset: IM |
Affiliation:
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Department of Physics, Boston University, Boston, Massachusetts 02215, USA. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Electricity Hemolysin Proteins / chemistry, metabolism Kinetics Models, Molecular Molecular Conformation* Nanostructures / chemistry Poly A / chemistry*, metabolism Porosity Proteins / chemistry*, metabolism RNA / chemistry, metabolism Temperature Thermodynamics Time Factors |
| Chemical | |
Reg. No./Substance:
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0/Hemolysin Proteins; 0/Proteins; 24937-83-5/Poly A; 63231-63-0/RNA |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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