Helix-coil kinetics of individual polyadenylic acid molecules in a protein channel.
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.
Lin
Jianxun
J
Department of Physics, Boston University, Boston, Massachusetts 02215, USA.
Kolomeisky
Anatoly
A
Meller
Amit
A
D004560:Electricity; D006460:Hemolysin Proteins / Q000737:chemistry / Q000378:metabolism; D007700:Kinetics; D008958:Models, Molecular; D008968:Molecular Conformation; D049329:Nanostructures / Q000737:chemistry; D011061:Poly A / Q000737:chemistry* / Q000378:metabolism; D016062:Porosity; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism; D012313:RNA / Q000737:chemistry / Q000378:metabolism; D013696:Temperature; D013816:Thermodynamics; D013997:Time Factors
D006460:Hemolysin Proteins; D011506:Proteins; D011061:Poly A; D012313:RNA