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Article: Direct detection of the formation of V-amylose helix by single molecule force spectroscopy

TitleDirect detection of the formation of V-amylose helix by single molecule force spectroscopy
Authors
Issue Date2006
PublisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/journals/jacsat/index.html
Citation
Journal Of The American Chemical Society, 2006, v. 128 n. 29, p. 9387-9393 How to Cite?
AbstractAn important polysaccharide, amylose crystallizes as a regular single left-handed helix from a propanol, butanol, or iodine solution. However, its solution structure remains elusive because amylose does not form molecular solutions in these solvents, and standard spectroscopic techniques cannot be exploited to determine its structure. Using AFM, we forced individual amylose chains adsorbed to a surface to enter these poor solvents and carried out stretch-release measurements on them in solution. In this manner, we directly captured the formation of individual amylose helices induced by butanol and iodine. With an accuracy approaching that of X-ray diffraction on amylose crystals, we determined that the pitch of the helix in solution is 1.3 Å/ring. We also directly measured the force driving the formation of the helix in solution to be 50 pN. SMD simulations in explicit butanol reproduced the AFM-measured force-extension curves and revealed that the long plateau feature is caused by the rupture of O(2) n-O(6) n+6 and O(3) n-O(6) n+6 hydrogen bonds and by the unwinding of the helix. We also found that amylose helices formed in iodine solution are more compliant and hysteretic as compared to helices in butanol, which extend/relax reversibly. In iodine solution, the formation of the helix is inhibited by force and limited by the slow kinetics of the amylose-iodine complex. By forcing individual molecules into poor solvents and performing force spectroscopy measurements in solution, our AFM approach uniquely supplements X-ray diffraction and NMR methods for investigating solution conformations of insoluble biopolymers. © 2006 American Chemical Society.
Persistent Identifierhttp://hdl.handle.net/10722/168032
ISSN
2015 Impact Factor: 13.038
2015 SCImago Journal Rankings: 7.123
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorZhang, Qen_US
dc.contributor.authorLu, Zen_US
dc.contributor.authorHu, Hen_US
dc.contributor.authorYang, Wen_US
dc.contributor.authorMarszalek, PEen_US
dc.date.accessioned2012-10-08T03:14:23Z-
dc.date.available2012-10-08T03:14:23Z-
dc.date.issued2006en_US
dc.identifier.citationJournal Of The American Chemical Society, 2006, v. 128 n. 29, p. 9387-9393en_US
dc.identifier.issn0002-7863en_US
dc.identifier.urihttp://hdl.handle.net/10722/168032-
dc.description.abstractAn important polysaccharide, amylose crystallizes as a regular single left-handed helix from a propanol, butanol, or iodine solution. However, its solution structure remains elusive because amylose does not form molecular solutions in these solvents, and standard spectroscopic techniques cannot be exploited to determine its structure. Using AFM, we forced individual amylose chains adsorbed to a surface to enter these poor solvents and carried out stretch-release measurements on them in solution. In this manner, we directly captured the formation of individual amylose helices induced by butanol and iodine. With an accuracy approaching that of X-ray diffraction on amylose crystals, we determined that the pitch of the helix in solution is 1.3 Å/ring. We also directly measured the force driving the formation of the helix in solution to be 50 pN. SMD simulations in explicit butanol reproduced the AFM-measured force-extension curves and revealed that the long plateau feature is caused by the rupture of O(2) n-O(6) n+6 and O(3) n-O(6) n+6 hydrogen bonds and by the unwinding of the helix. We also found that amylose helices formed in iodine solution are more compliant and hysteretic as compared to helices in butanol, which extend/relax reversibly. In iodine solution, the formation of the helix is inhibited by force and limited by the slow kinetics of the amylose-iodine complex. By forcing individual molecules into poor solvents and performing force spectroscopy measurements in solution, our AFM approach uniquely supplements X-ray diffraction and NMR methods for investigating solution conformations of insoluble biopolymers. © 2006 American Chemical Society.en_US
dc.languageengen_US
dc.publisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/journals/jacsat/index.htmlen_US
dc.relation.ispartofJournal of the American Chemical Societyen_US
dc.subject.meshAmylose - Analogs & Derivatives - Chemistryen_US
dc.subject.meshButanols - Chemistryen_US
dc.subject.meshCarbohydrate Conformationen_US
dc.subject.meshIodine - Chemistryen_US
dc.subject.meshMolecular Structureen_US
dc.subject.meshSolutionsen_US
dc.subject.meshSolvents - Chemistryen_US
dc.subject.meshSpectrum Analysis - Methodsen_US
dc.subject.meshWater - Chemistryen_US
dc.titleDirect detection of the formation of V-amylose helix by single molecule force spectroscopyen_US
dc.typeArticleen_US
dc.identifier.emailHu, H:haohu@hku.hken_US
dc.identifier.authorityHu, H=rp00707en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1021/ja057693+en_US
dc.identifier.pmid16848474-
dc.identifier.scopuseid_2-s2.0-33746368406en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-33746368406&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume128en_US
dc.identifier.issue29en_US
dc.identifier.spage9387en_US
dc.identifier.epage9393en_US
dc.identifier.isiWOS:000239120700052-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridZhang, Q=7406720998en_US
dc.identifier.scopusauthoridLu, Z=36708080000en_US
dc.identifier.scopusauthoridHu, H=7404097564en_US
dc.identifier.scopusauthoridYang, W=7407757509en_US
dc.identifier.scopusauthoridMarszalek, PE=7003447079en_US

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