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Article: NMR studies of metalloproteins

TitleNMR studies of metalloproteins
Authors
Issue Date2012
PublisherSpringer Verlag.
Citation
Topics in Current Chemistry, 2012, v. 326, p. 69-98 How to Cite?
AbstractMetalloproteins represent a large share of the proteomes, with the intrinsic metal ions providing catalytic, regulatory, and structural roles critical to protein functions. Structural characterization of metalloproteins and identification of metal coordination features including numbers and types of ligands and metal-ligand geometry, and mapping the structural and dynamic changes upon metal binding are significant for understanding biological functions of metalloproteins. NMR spectroscopy has long been used as an invaluable tool for structure and dynamic studies of macromolecules. Here we focus on the application of NMR spectroscopy in characterization of metalloproteins, including structural studies and identification of metal coordination spheres by hetero-/homo-nuclear metal NMR spectroscopy. Paramagnetic NMR as well as (13)C directly detected protonless NMR spectroscopy will also be addressed for application to paramagnetic metalloproteins. Moreover, these techniques offer great potential for studies of other non-metal binding macromolecules.
Persistent Identifierhttp://hdl.handle.net/10722/142327
ISSN
2015 Impact Factor: 4.014
2015 SCImago Journal Rankings: 1.144
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorLi, Hen_US
dc.contributor.authorSun, Hen_US
dc.date.accessioned2011-10-28T02:43:11Z-
dc.date.available2011-10-28T02:43:11Z-
dc.date.issued2012en_US
dc.identifier.citationTopics in Current Chemistry, 2012, v. 326, p. 69-98en_US
dc.identifier.issn0340-1022en_US
dc.identifier.urihttp://hdl.handle.net/10722/142327-
dc.description.abstractMetalloproteins represent a large share of the proteomes, with the intrinsic metal ions providing catalytic, regulatory, and structural roles critical to protein functions. Structural characterization of metalloproteins and identification of metal coordination features including numbers and types of ligands and metal-ligand geometry, and mapping the structural and dynamic changes upon metal binding are significant for understanding biological functions of metalloproteins. NMR spectroscopy has long been used as an invaluable tool for structure and dynamic studies of macromolecules. Here we focus on the application of NMR spectroscopy in characterization of metalloproteins, including structural studies and identification of metal coordination spheres by hetero-/homo-nuclear metal NMR spectroscopy. Paramagnetic NMR as well as (13)C directly detected protonless NMR spectroscopy will also be addressed for application to paramagnetic metalloproteins. Moreover, these techniques offer great potential for studies of other non-metal binding macromolecules.en_US
dc.languageengen_US
dc.publisherSpringer Verlag.en_US
dc.relation.ispartofTopics in Current Chemistryen_US
dc.rightsThe original publication is available at www.springerlink.comen_US
dc.rightsCreative Commons: Attribution 3.0 Hong Kong License-
dc.subject.meshCarbon Isotopes - diagnostic use-
dc.subject.meshHumans-
dc.subject.meshMetalloproteins - chemistry-
dc.subject.meshNuclear Magnetic Resonance, Biomolecular - methods-
dc.titleNMR studies of metalloproteinsen_US
dc.typeArticleen_US
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0340-1022&volume=128&spage=&epage=&date=2011&atitle=NMR+studies+of+metalloproteinsen_US
dc.identifier.emailLi, H: hylichem@hku.hken_US
dc.identifier.emailSun, H: hsun@hku.hken_US
dc.identifier.authoritySun, H=rp00777en_US
dc.description.naturepostprint-
dc.identifier.doi10.1007/128_2011_214en_US
dc.identifier.pmid21809188-
dc.identifier.scopuseid_2-s2.0-84859926387-
dc.identifier.hkuros205088en_US
dc.identifier.volume326en_US
dc.identifier.spage69-
dc.identifier.epage98-
dc.identifier.isiWOS:000321618300005-
dc.publisher.placeGermany-

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