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dc.contributor.author이은규-
dc.date.accessioned2019-05-23T04:47:33Z-
dc.date.available2019-05-23T04:47:33Z-
dc.date.issued2016-08-
dc.identifier.citationJOURNAL OF MOLECULAR RECOGNITION, v. 29, No. 9, Page. 446-451en_US
dc.identifier.issn0952-3499-
dc.identifier.issn1099-1352-
dc.identifier.urihttps://onlinelibrary.wiley.com/doi/full/10.1002/jmr.2543-
dc.identifier.urihttps://repository.hanyang.ac.kr/handle/20.500.11754/105901-
dc.description.abstractA fluorescent reporter, 8-anilino-1-naphthalene sulfonic acid (ANS), can serve as a reference molecule for conformational transition of a protein because its aromatic carbons have strong affinity with hydrophobic cores of partially unfolded molten globules. Using a typical calcium-binding protein, bovine -lactalbumin (BLA), as a model protein, we compared the ANS binding thermodynamics to the decalcified (10mM EDTA treated) apo-BLA at two representative temperatures: 20 and 40 degrees C. This is because the authentic molten globule is known to form more heavily at an elevated temperature such as 40 degrees C. Isothermal titration calorimetry experiments revealed that the BLA-ANS interactions at both temperatures were entropy-driven, and the dissociation constants were similar on the order of 10(-4)M, but there was a dramatic changeover in the binding thermodynamics from endothermic at 20 degrees C to exothermic at 40 degrees C. We believe that the higher subpopulation of authentic molten globules at 40 degrees C than 20 degrees C would be responsible for the results, which also indicate that weak binding is sufficient to alter the ANS binding mechanisms. We expect that the thermodynamic properties obtained from this study would serve as a useful reference for investigating the binding of other hydrophobic ligands such as oleic acid to apo-BLA, because oleic acid is known to have tumor-selective cytotoxicity when complexed with partially unfolded -lactalbumin. Copyright (c) 2016 John Wiley Sons, Ltd.en_US
dc.description.sponsorshipThis research was supported by Basic Science Research Program through the National Research Foundation of Korea (NRF) funded by the Ministry of Science, ICT and Future Planning (No. 2008‐0061891).en_US
dc.language.isoen_USen_US
dc.publisherWILEY-BLACKWELLen_US
dc.subjectbovine -lactalbuminen_US
dc.subjectANSen_US
dc.subjectbinding thermodynamicsen_US
dc.subjectfluorescence spectroscopyen_US
dc.subjectITCen_US
dc.subjectmolten globuleen_US
dc.titleThermodynamic analysis of ANS binding to partially unfolded -lactalbumin: correlation of endothermic to exothermic changeover with formation of authentic molten globulesen_US
dc.typeArticleen_US
dc.relation.no9-
dc.relation.volume29-
dc.identifier.doi10.1002/jmr.2543-
dc.relation.page446-451-
dc.relation.journalJOURNAL OF MOLECULAR RECOGNITION-
dc.contributor.googleauthorKim, Ki Hyung-
dc.contributor.googleauthorYun, Soi-
dc.contributor.googleauthorMok, K. H.-
dc.contributor.googleauthorLee, E. K.-
dc.relation.code2016001586-
dc.sector.campusE-
dc.sector.daehakCOLLEGE OF ENGINEERING SCIENCES[E]-
dc.sector.departmentDEPARTMENT OF BIONANO ENGINEERING-
dc.identifier.pideklee-
Appears in Collections:
COLLEGE OF ENGINEERING SCIENCES[E](공학대학) > BIONANO ENGINEERING(생명나노공학과) > Articles
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