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Partitioning of a polymer into a nanoscopic protein pore obeys a simple scaling law

The dependence of the rate on polymer mass was examined for the reaction of four sulfhydryl-directed poly(ethylene glycol) reagents with cysteine residues located in the lumen of the staphylococcal α-hemolysin pore. The logarithms of the apparent rate constants for a particular site in the lumen wer...

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Автори: Movileanu, Liviu, Bayley, Hagan
Формат: Стаття
Мова:en
Опубліковано: The National Academy of Sciences 2001
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Онлайн доступ:https://ncbi.nlm.nih.gov/pmc/articles/PMC56928/
https://ncbi.nlm.nih.gov/pubmed/11504913
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.181089798
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spelling pubmed-569282001-10-01 Partitioning of a polymer into a nanoscopic protein pore obeys a simple scaling law Movileanu, Liviu Bayley, Hagan Proc Natl Acad Sci U S A Biological Sciences The dependence of the rate on polymer mass was examined for the reaction of four sulfhydryl-directed poly(ethylene glycol) reagents with cysteine residues located in the lumen of the staphylococcal α-hemolysin pore. The logarithms of the apparent rate constants for a particular site in the lumen were proportional to N, the number of repeat units in a polymer chain. The proportionality constant was −(a/D)(5/3), where a is the persistence length of the polymer (≈3.5Å) and D is the diameter of the pore. Despite some incongruencies with the assumptions of the derivation, the result suggests that the polymers partition into the lumen of the pore according to the simple scaling law of Daoud and de Gennes, c(pore)/c(solution) = exp(−N(a/D)(5/3)). Therefore, the measured reaction rates yield an estimate of the diameter of the pore and might be applied to determine the approximate dimensions of cavities within other similar proteins. The National Academy of Sciences 2001-08-28 2001-08-14 /pmc/articles/PMC56928/ /pubmed/11504913 http://dx.doi.org/10.1073/pnas.181089798 Text en Copyright © 2001, The National Academy of Sciences
institution US National Library of Medicine
collection PubMed Central
language en
format Article
topic Biological Sciences
spellingShingle Biological Sciences
Movileanu, Liviu
Bayley, Hagan
Partitioning of a polymer into a nanoscopic protein pore obeys a simple scaling law
description The dependence of the rate on polymer mass was examined for the reaction of four sulfhydryl-directed poly(ethylene glycol) reagents with cysteine residues located in the lumen of the staphylococcal α-hemolysin pore. The logarithms of the apparent rate constants for a particular site in the lumen were proportional to N, the number of repeat units in a polymer chain. The proportionality constant was −(a/D)(5/3), where a is the persistence length of the polymer (≈3.5Å) and D is the diameter of the pore. Despite some incongruencies with the assumptions of the derivation, the result suggests that the polymers partition into the lumen of the pore according to the simple scaling law of Daoud and de Gennes, c(pore)/c(solution) = exp(−N(a/D)(5/3)). Therefore, the measured reaction rates yield an estimate of the diameter of the pore and might be applied to determine the approximate dimensions of cavities within other similar proteins.
author Movileanu, Liviu
Bayley, Hagan
author_facet Movileanu, Liviu
Bayley, Hagan
author_sort Movileanu, Liviu
title Partitioning of a polymer into a nanoscopic protein pore obeys a simple scaling law
title_short Partitioning of a polymer into a nanoscopic protein pore obeys a simple scaling law
title_full Partitioning of a polymer into a nanoscopic protein pore obeys a simple scaling law
title_fullStr Partitioning of a polymer into a nanoscopic protein pore obeys a simple scaling law
title_full_unstemmed Partitioning of a polymer into a nanoscopic protein pore obeys a simple scaling law
title_sort partitioning of a polymer into a nanoscopic protein pore obeys a simple scaling law
publisher The National Academy of Sciences
publisher_facet The National Academy of Sciences
publishDate 2001
url https://ncbi.nlm.nih.gov/pmc/articles/PMC56928/
https://ncbi.nlm.nih.gov/pubmed/11504913
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.181089798
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