Results 51 to 60 of about 14,646 (214)

NMR Studies of Metalloproteins [PDF]

open access: yes, 2011
Metalloproteins 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 ...
Sun, H, Li, H
openaire   +4 more sources

Protein‐Driven Copper Redox Regulation: Uncovering the Role of Disulphide Bonds and Allosteric Modulation

open access: yesAngewandte Chemie International Edition, EarlyView.
Copper binding triggers structural changes that expose a reactive disulphide bridge, enabling intrinsic Cu(II) reduction in folded proteins. SAXS, XAS, and QM/MM simulations reveal how globular proteins such as HSA and SOD1 employ disulphide‐mediated dynamics to modulate site accessibility and control copper redox chemistry.
Rebecca Sternke‐Hoffmann   +9 more
wiley   +1 more source

Metal Complexes of Macrocyclic Ligands

open access: yesCHIMIA, 1999
Metal complexes of macrocyclic ligands are studied with a view to understanding aspects of metalloprotein structure and function.
Thomas A. Kaden
doaj   +1 more source

Immunization of mice with the self-peptide ACBP coupled to keyhole limpet hemocyanin

open access: yesSTAR Protocols, 2022
Summary: Keyhole limpet hemocyanin (KLH) is a glycosylated multi-subunit metalloprotein that elicits a strong nonspecific immune activation, thus inducing both cellular and humoral immune responses.
Léa Montégut   +5 more
doaj   +1 more source

Probing metal ion binding and conformational properties of the colicin E9 endonuclease by electrospray ionization time-of-flight mass spectrometry [PDF]

open access: yes, 2002
Nano-electrospray ionization time-of-flight mass spectrometry (ESI-MS) was used to study the conformational consequences of metal ion binding to the colicin E9 endonuclease (E9 DNase) by taking advantage of the unique capability of ESI-MS to allow ...
HECK, ALBERT J.R.   +6 more
core   +3 more sources

Cu(I) Is a Game Changer in the Arrest of Cu(Aβ)‐Induced ROS Production in the Presence of Competing Zn(II) Ions

open access: yesChemistry – A European Journal, EarlyView.
ABSTRACT ROS production due to Cu(amyloid‐β) redox cycling is proposed to contribute to the oxidative stress observed in Alzheimer's disease brains. We previously reported on a nitrogen and sulfur‐containing ligand, L, able to arrest Cu(Aβ)‐induced ROS production [Chem. Eur. J. 2023, 29,].
Marielle Drommi   +4 more
wiley   +1 more source

Machine Learning Approaches for Metalloproteins

open access: yesMolecules, 2022
Metalloproteins are a family of proteins characterized by metal ion binding, whereby the presence of these ions confers key catalytic and ligand-binding properties.
Yue Yu, Ruobing Wang, Ruijie D. Teo
doaj   +1 more source

Quantitative Competition Binding of Fluorinated Ligands by Real‐Time 19F In‐Cell NMR to Assess Isoform Selectivity in Human Cells

open access: yesMagnetic Resonance in Chemistry, EarlyView.
Real‐time in‐cell 19F NMR spectroscopy in a flow NMR bioreactor was used to monitor the binding of fluorinated compounds to three cytosolic carbonic anhydrase isoforms in living human cells. The simultaneous observation of the two ligands allowed for the quantitative ranking of their intracellular affinities by competition binding. This approach allows
Azzurra Costantino   +5 more
wiley   +1 more source

An investigation into the feasibility of myoglobin-based single-electron transistors

open access: yes, 2012
Myoglobin single-electron transistors were investigated using nanometer- gap platinum electrodes fabricated by electromigration at cryogenic temperatures. Apomyoglobin (myoglobin without heme group) was used as a reference.
Bendall D S   +9 more
core   +1 more source

Imaging of compartmentalised intracellular nitric oxide, induced during bacterial phagocytosis, using a metalloprotein–gold nanoparticle conjugate [PDF]

open access: yes, 2017
Nitric oxide (NO) plays an essential role within the immune system since it is involved in the break-down of infectious agents such as viruses and bacteria.
Gavrilovic, Jelena   +4 more
core   +1 more source

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