Results 151 to 160 of about 27,575 (332)

Metalloprotein-based electronic nanodevices [PDF]

, 2006
A key challenge of the current research in nanoelectronics is the realization of biomolecular devices. The use of electron-transfer proteins, such as the blue copper protein, azurin (Az), is particularly attractive because of its natural redox properties and self-assembly capability.
RINALDI, Rosaria, MARUCCIO, Giuseppe, BIASCO, Adriana Lucia Angela, POMPA, Pier Paolo, A. Bramanti, ARIMA, VALENTINA, VISCONTI, Paolo, D'AMICO, STEFANO, E. D'Amone, CINGOLANI, Roberto   +9 more
openaire   +5 more sources

Fluorescent binary ensemble with pattern recognition ability for identifying multiple metalloproteins with applications in serum and urine

, 2017
Discrimination and identification of multiple metalloproteins by a single sensor system are challenging. Based on the strategy of surfactant assembly modulation effect, a strong discriminative sensor based on a pyrene-derived fluorophore and an anionic ...
Demin Zheng, Junmei Fan, Xinyan Huang, Liping Ding, Yunhong Xin   +4 more
semanticscholar   +1 more source

A less‐biased analysis of metalloproteins reveals novel zinc coordination geometries

Proteins: Structure, Function, and Bioinformatics, 2015
Zinc metalloproteins are involved in many biological processes and play crucial biochemical roles across all domains of life. Local structure around the zinc ion, especially the coordination geometry (CG), is dictated by the protein sequence and is often
Sen Yao, R. Flight, E. Rouchka, H. Moseley   +3 more
semanticscholar   +1 more source

The Role of Asparagine as a Gatekeeper Residue in the Selective Binding of Rare Earth Elements by Lanthanide‐Binding Peptides

Chemistry – A European Journal, Volume 31, Issue 33, June 12, 2025.
Lanthanide binding tags (LBTs) have been utilized as a green extractant to selectively separate rare earth elements (REEs). We reveal up from the molecular level how the N5 asparagine residue is indispensable in imparting selective complexation between lighter and heavier lanthanides by conformationally functioning as a gate.
Surabh S. KT, Baofu Qiao, Jason G. Marmorstein, Yiming Wang, Denize C. Favaro, Kathleen J. Stebe, E. James Petersson, Ravi Radhakrishnan, Cesar de la Fuente‐Nunez, Raymond S. Tu, Charles Maldarelli, Monica Olvera de la Cruz, Robert J. Messinger   +12 more
wiley   +1 more source

Waltzing around cofactors

eLife, 2016
The metallocofactor involved in fixing nitrogen is not a rigid scaffold, as was previously thought.
Percival Yang-Ting Chen, Elizabeth C Wittenborn, Catherine L Drennan   +2 more
doaj   +1 more source

EPR of Co(II) as a Structural and Mechanistic Probe of Metalloprotein Active Sites: A Review of Studies on Aminopeptidase [PDF]

, 2002
Co(II) can often be substituted for Zn(II) in zinc-dependent metalloenzymes to provide spectroscopically accessible forms of the enzymes. Co(II) is an excellent spectroscopic probe as it is both optically active and EPR active.
Bennett, Brian
core   +1 more source

Studies on the conformational changes of metalloproteins induced by electrons in water—ethylene glycol solutions at low temperatures. Cytochrome C [PDF]

, 1974
Lev Blumenfeld, Roman Davydov, N.S. Fel', S. N. Magonov, Raivo Vilu   +4 more
openalex   +1 more source

Purine Chemistry in the Early RNA World at the Origins of Life: From RNA and Nucleobases Lesions to Current Key Metabolic Routes

ChemBioChem, Volume 26, Issue 11, June 3, 2025.
In the nascent processes of the beginnings and evolution of life, nucleobases and especially purines, ribonucleos(t)ides and primitive RNAs have been continuously modified. A RNA‐peptide world and key metabolic pathways probably have emerged from the corresponding chemical modifications resulting from adenine deamination, purine alkylation and ...
Jean‐Luc Décout, Marie‐Christine Maurel   +1 more
wiley   +1 more source

Probing metalloproteins by voltammetry [PDF]

, 2006
Dynamic electrochemical methods, which have long held an important place among the techniques of the coordination chemist, have generally remained unexploited by those seeking to understand the complex and often elusive chemistry of metal centres in proteins.
openaire   +2 more sources

Hidden relationships between metalloproteins unveiled by structural comparison of their metal sites

Scientific Reports, 2015
Metalloproteins account for a substantial fraction of all proteins. They incorporate metal atoms, which are required for their structure and/or function.
Yana Valasatava, Claudia Andreini, A. Rosato   +2 more
semanticscholar   +1 more source