Detailed Information

Cited 0 time in webofscience Cited 0 time in scopus
Metadata Downloads

NMR Studies of Metal-binding Luteinizing Hormone Releasing Hormone

Full metadata record
DC Field Value Language
dc.contributor.authorWon, Hoshik-
dc.date.accessioned2021-06-23T10:05:07Z-
dc.date.available2021-06-23T10:05:07Z-
dc.date.issued2011-11-
dc.identifier.issn0253-2964-
dc.identifier.issn1229-5949-
dc.identifier.urihttps://scholarworks.bwise.kr/erica/handle/2021.sw.erica/36401-
dc.description.abstractFunctions of the luteinizing hormone releasing hormone (LHRH) and its induced release by divalent metal ions have received great attention because this neurotransmitter subsequently regulates the secretion of luteinizing hormone (LH). Metal-LHRH complexes were synthesized by addition of various Cu(II),Ni(II),Zn(II) ions into LHRH in order to understand how the induced release of LHRH is possible. The degree of complexation was monitored by H-1, C-13-NMR chemical shifts, and final products were identified by Mass spectrometry. Solution-state structure determination of Zn(II)-LHRH out of metal-complexes was accomplished by using NMR and NMR-based distance geometry (DG). Interproton distance information from nuclear Overhauser effect spectroscopy was utilized for structure determination. Structure obtained in this study has a cyclic conformation exhibiting a specific a-helical turn with residue numbers His[2]-Leu[7] out of 10 amino acids. Comparison of chemical shifts and EPR studies of Ni(II),Cu(IT)-LHRH complexes exhibit that these metal complexes have 4-coordination geometry.-
dc.format.extent6-
dc.language영어-
dc.language.isoENG-
dc.publisher대한화학회-
dc.titleNMR Studies of Metal-binding Luteinizing Hormone Releasing Hormone-
dc.typeArticle-
dc.publisher.location대한민국-
dc.identifier.doi10.5012/bkcs.2011.32.11.4021-
dc.identifier.scopusid2-s2.0-81755173002-
dc.identifier.wosid000297398800033-
dc.identifier.bibliographicCitationBulletin of the Korean Chemical Society, v.32, no.11, pp 4021 - 4026-
dc.citation.titleBulletin of the Korean Chemical Society-
dc.citation.volume32-
dc.citation.number11-
dc.citation.startPage4021-
dc.citation.endPage4026-
dc.type.docTypeArticle-
dc.identifier.kciidART001601666-
dc.description.isOpenAccessN-
dc.description.journalRegisteredClasssci-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
dc.description.journalRegisteredClasskci-
dc.relation.journalResearchAreaChemistry-
dc.relation.journalWebOfScienceCategoryChemistry, Multidisciplinary-
dc.subject.keywordPlusANGIOTENSIN-CONVERTING ENZYME-
dc.subject.keywordPlusBIOLOGICAL-ACTIVITY-
dc.subject.keywordPlusPORCINE LH-
dc.subject.keywordPlusCOMPLEXES-
dc.subject.keywordPlusRECEPTOR-
dc.subject.keywordPlusCOENZYME-F430-
dc.subject.keywordPlusANTAGONISTS-
dc.subject.keywordPlusCOPPER(II)-
dc.subject.keywordPlusMETABOLISM-
dc.subject.keywordPlusPEPTIDE-
dc.subject.keywordAuthorNMR-
dc.subject.keywordAuthorLHRH-
dc.subject.keywordAuthorMetal-LHRH complex-
dc.identifier.urlhttp://koreascience.or.kr/article/JAKO201101152704704.page-
Files in This Item
Go to Link
Appears in
Collections
COLLEGE OF SCIENCE AND CONVERGENCE TECHNOLOGY > DEPARTMENT OF CHEMICAL AND MOLECULAR ENGINEERING > 1. Journal Articles

qrcode

Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.

Related Researcher

Researcher Won, Ho shik photo

Won, Ho shik
ERICA 공학대학 (ERICA 에너지바이오학과)
Read more

Altmetrics

Total Views & Downloads

BROWSE