Structure and dynamics of heme proteins

Banci, Lucia

doi:10.1002/(sici)1099-1409(200006/07)4:4<390::aid-jpp255>3.0.co;2-n

Cited by 3 publications

(3 citation statements)

References 56 publications

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“…incorporated paramagnetic Cu(II) at selected sites in the protein as a paramagnetic relaxation enhancement agent to study long‐range structural restraints in proteins using solid‐state NMR . It should be noted that the resonance line broadening of the surrounding nuclei due to paramagnetic metal ions with fast electronic relaxation is limited compared with the broadening caused by metal ions with long electronic relaxation . For example, iron ions have fast electronic relaxation.…”

Section: Nmr Spectroscopymentioning

confidence: 99%

“…[218] It should be noted that the resonance line broadening of the surrounding nuclei due to paramagnetic metal ions with fast electronic relaxation is limited compared with the broadening caused by metal ions with long electronic relaxation. [219,220] For example, iron ions have fast electronic relaxation. NMR signals of atoms close to iron in heme can thus be detected leading to structural determination of several heme proteins.…”

Section: Paramagnetic Nmr Spectroscopymentioning

confidence: 99%

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Utilizing NMR and EPR spectroscopy to probe the role of copper in prion diseases

Emwas

Al‐Talla

Guo

et al. 2013

Magnetic Reson in Chemistry

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Copper is an essential nutrient for the normal development of the brain and nervous system, although the hallmark of several neurological diseases is a change in copper concentrations in the brain and central nervous system. Prion protein (PrP) is a copper-binding, cell-surface glycoprotein that exists in two alternatively folded conformations: a normal isoform (PrP(C)) and a disease-associated isoform (PrP(Sc)). Prion diseases are a group of lethal neurodegenerative disorders that develop as a result of conformational conversion of PrP(C) into PrP(Sc). The pathogenic mechanism that triggers this conformational transformation with the subsequent development of prion diseases remains unclear. It has, however, been shown repeatedly that copper plays a significant functional role in the conformational conversion of prion proteins. In this review, we focus on current research that seeks to clarify the conformational changes associated with prion diseases and the role of copper in this mechanism, with emphasis on the latest applications of NMR and EPR spectroscopy to probe the interactions of copper with prion proteins.

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Section: Nmr Spectroscopymentioning

confidence: 99%

Section: Paramagnetic Nmr Spectroscopymentioning

confidence: 99%

Utilizing NMR and EPR spectroscopy to probe the role of copper in prion diseases

Emwas

Al‐Talla

Guo

et al. 2013

Magnetic Reson in Chemistry

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“…For this reason, in heme proteins even the signals close to the iron can be observed, and a considerable number of structures has been solved. Because several recent reviews dealing with heme proteins are available (8,14,30,86,120), these will not be discussed here. It has been possible to solve several solution structures even for proteins with metals that cause more significant broadening, such as FeS proteins (28).…”

Section: Structure Determination Of Paramagnetic Macromoleculesmentioning

confidence: 99%

Paramagnetic Resonance of Biological Metal Centers

Ubbink

Worrall²,

Canters³

et al. 2002

Annu. Rev. Biophys. Biomol. Struct.

109

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The review deals with recent advances in magnetic resonance spectroscopy (hf EPR and NMR) of paramagnetic metal centers in biological macromolecules. In the first half of our chapter, we present an overview of recent technical developments in the NMR of paramagnetic bio-macromolecules. These are illustrated by a variety of examples deriving mainly from the spectroscopy of metalloproteins and their complexes. The second half focuses on recent developments in high-frequency EPR spectroscopy and the application of the technique to copper, iron, and manganese proteins. Special attention is given to the work on single crystals of copper proteins.

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Layered double hydroxides functionalized with anionic surfactant: Direct electrochemistry and electrocatalysis of hemoglobin

Chen

et al. 2008

Electrochimica Acta

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Structure and dynamics of heme proteins

Cited by 3 publications

References 56 publications

Utilizing NMR and EPR spectroscopy to probe the role of copper in prion diseases

Utilizing NMR and EPR spectroscopy to probe the role of copper in prion diseases

Paramagnetic Resonance of Biological Metal Centers

Layered double hydroxides functionalized with anionic surfactant: Direct electrochemistry and electrocatalysis of hemoglobin

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