Results 61 to 70 of about 21,602 (293)
ChemBioChem, EarlyView.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 +1 more
wiley +1 more source
IUCrJ, 2016 Lytic polysaccharide monooxygenases (LPMOs) are a new class of microbial copper enzymes involved in the degradation of recalcitrant polysaccharides.
Kristian E. H. Frandsen, Leila Lo Leggio
doaj +1 more source
Joint Design of Protein Sequence and Structure based on Motifs [PDF]
arXiv, 2023 Designing novel proteins with desired functions is crucial in biology and chemistry. However, most existing work focus on protein sequence design, leaving protein sequence and structure co-design underexplored. In this paper, we propose GeoPro, a method to design protein backbone structure and sequence jointly.
arxiv
Electron paramagnetic resonance spectroscopy using a single artificial atom [PDF]
Commun Phys 2, 33 (2019), 2017 Electron paramagnetic resonance (EPR) spectroscopy is an important technology in physics, chemistry, materials science, and biology. Sensitive detection with a small sample volume is a key objective in these areas, because it is crucial, for example, for the readout of a highly packed spin based quantum memory or the detection of unlabeled ...
arxiv +1 more source
Designing Enzymatic Reactivity with an Expanded Palette
ChemBioChem, EarlyView.Innovation in biocatalysis is rapidly increasingly the diversity of catalytic reactivity that can be mediated by enzymes, addressing a key bottleneck for their widespread adoption in industrial chemical synthesis. A key approach to this is building enzymes with unnatural catalytic components that provide an expanded palette with new possibilities for ...
Reuben B. Leveson‐Gower
wiley +1 more source
AIMS Biophysics, 2018 The constant increase of computational power has made feasible to investigate the folding mechanism of small proteins using molecular dynamics (MD). Metal-binding proteins (metalloproteins) are usually complicated to model, largely due to the presence of
Davide Sala +2 more
doaj +1 more source
How many metals does it take to fix N2? A mechanistic overview of biological nitrogen fixation [PDF]
, 2006 During the process of biological nitrogen fixation, the enzyme nitrogenase catalyzes the ATP-dependent reduction of dinitrogen to ammonia. Nitrogenase consists of two component metalloproteins, the iron (Fe) protein and the molybdenum-iron (MoFe) protein;
Howard, James B., Rees, Douglas C.
core +1 more source
Exploiting SpyTag/SpyCatcher Technology to Design New Artificial Catalytic Copper Proteins
ChemBioChem, EarlyView.Designing artificial metal sites in proteins is challenging due to the need to place the metal site in precise positions and to tailor the coordination environment of the metal. A modular approach based on the SpyTag/SpyCatcher technology is used to provide the Spy construct with a Cu2+/ATCUN site.
Silvia Gentili +11 more
wiley +1 more source
Reflections on the Origin of Coded Protein Biosynthesis
BiomoleculesThe principle of continuity posits that some central features of primordial biocatalytic mechanisms should still be present in the genetically dependent pathway of protein synthesis, a crucial step in the emergence of life.
Juan Carlos Fontecilla-Camps
doaj +1 more source
Magnetochemistry, 2020 The study of cellular machineries responsible for the iron–sulfur (Fe–S) cluster biogenesis has led to the identification of a large number of proteins, whose importance for life is documented by an increasing number of diseases linked to them.
Mario Piccioli
doaj +1 more source