Results 101 to 110 of about 6,022 (216)

Surface Plasmon Resonance Sensing of Biorecognition Interactions within the Tumor Suppressor p53 Network

Sensors, 2017
Surface Plasmon Resonance (SPR) is a powerful technique to study the kinetics of biomolecules undergoing biorecognition processes, particularly suited for protein-protein interactions of biomedical interest. The potentiality of SPR was exploited to sense
Ilaria Moscetti, Salvatore Cannistraro, Anna Rita Bizzarri   +2 more
doaj   +1 more source

A Spectroscopic and Calorimetric Investigation on the Thermal Stability of the Cys3Ala/Cys26Ala Azurin Mutant

, 1999
The disulfide bond connecting Cys-3 and Cys-26 in wild type azurin has been removed to study the contribution of the –SS– bond to the high thermal resistance previously registered for this protein (La Rosa et al. 1995. J. Phys. Chem.
Grasso, D., Milardi, D., Canters, G.W., La Rosa, C., Rosa, C. la, Guzzi, R., Sportelli, L., Verbeet, M.P., Verbeet, M. Ph.   +8 more
core   +1 more source

Electron-transfer properties of Pseudomonas aeruginosa [Lys44, Glu64]azurin

, 1997
In the hydrophobic patch of azurin from Pseudomonas aeruginosa, an electric dipole was created by changing Met44 into Lys and. Met64 into Glu, The effect of this dipole on the electron-transfer properties of azurin was investigated.
Pouderoyen, G., M. C. Silvestrini, Canters, G.W., Cigna, G., Malatesta, F., CUTRUZZOLA', Francesca, Cutruzzola, F., Rolli, G., G. Cigna, G. Rolli, Brunori, M., G. W. Canters, G. Van Pouderoyen, BRUNORI, Maurizio, Silvestrini, M.C., MALATESTA, FRANCESCO   +15 more
core   +1 more source

The role of His117 in the redox reactions of azurin from Pseudomonas aeruginosa

, 1996
The electron-transfer properties of H117G- and wild-type azurin were compared by applying both as electron acceptors in the conversion of 4-ethylphenol by 4-ethylphenol methylenehydroxylase (4-EPMH).
Tanneke den Blaauwen, Hopper, David J., Canters, G.W., Duine, J.A., Duine, Johannis A., David J. Hopper, Johannis A. Duine, Hopper, D.J., Gorren, A.C.F., Gorren, Antonius C.F., Gerard W. Canters, Blaauwen, T. den, Canters, Gerard W., Antonius C.F. Gorren, den Blaauwen, Tanneke   +14 more
core   +1 more source

A Pseudomonas aeruginosa type VI secretion system regulated by CueR facilitates copper acquisition.

PLoS Pathogens, 2019
The type VI secretion system (T6SS) is widely distributed in Gram-negative bacteria, whose function is known to translocate substrates to eukaryotic and prokaryotic target cells to cause host damage or as a weapon for interbacterial competition ...
Yuying Han, Tietao Wang, Gukui Chen, Qinqin Pu, Qiong Liu, Yani Zhang, Linghui Xu, Min Wu, Haihua Liang   +8 more
doaj   +1 more source

Lipid-Modified Azurin of Neisseria gonorrhoeae Is Not Surface Exposed and Does Not Interact With the Nitrite Reductase AniA

Frontiers in Microbiology, 2018
Lipid-modified cupredoxin azurin (Laz) is involved in electron transport in Neisseria and proposed to act as an electron donor to the surface-displayed nitrite reductase AniA.
Benjamin I. Baarda, Ryszard A. Zielke, Ann E. Jerse, Aleksandra E. Sikora, Aleksandra E. Sikora   +4 more
doaj   +1 more source

Click Chemistry with an Active Site Variant of Azurin

European Journal of Inorganic Chemistry, 2006
AbstractThe active site of the blue copper protein azurin (Azu) from Pseudomonas aeruginosa consists of a Cu ion immobilized by bonds to four amino acid side chains. The protein assists in electron transfer in vivo. Replacement of Cu‐ligand His117 by a Gly makes the Cu site accessible for exogenous ligands.
Jongh, T.E. de, Roon, A. van, Prudêncio, M., Ubbink, M., Canters, G.W.   +4 more
openaire   +2 more sources

Probing the roles of metal binding ligands in cupredoxins: incorporating nonproteinogenic amino acids into azurin and CuA Azurin

, 2010
Item withdrawn by Mark Zulauf (zulauf@illinois.edu) on 2010-05-13T19:03:20Z Item was in collections: University of Illinois Theses & Dissertations (ID: 1) No.
Clark, Kevin M.
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Circular permutants of azurin exhibit molten globule intermediates not observed in WT azurin

Abstract Molten globule (MG) states of proteins have been described as special types of intermediate states within the energy landscape diagram of proteins. In a cell, the MG state has functional significance compared to the native or unfolded states owing to its enhanced side-chain dynamics.
Debanjana Das, Sri Rama Koti Ainavarapu
openaire   +1 more source

Folding and Structure of Azurin - The Influence of a Metal

, 2001
The structural role of the metal in the protein azurin from Pseudomonas aeruginosa has been a long standing question. Azurin belongs to the cupredoxin family and is a 128 residue beta-barrel protein of greek-key topology.
Leckner, Johan
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