Results 201 to 210 of about 25,004 (307)

Insights into the catalytic mechanism of formate dehydrogenases from different microbial sources

open access: yesThe FEBS Journal, EarlyView.
This integrated study combines experimental enzyme kinetics with QM/MM simulations to map the catalytic mechanisms of four formate dehydrogenases at the atomic level. This approach reveals the key determinants of catalytic efficiency and guides the rational design of biocatalysts for effective CO2 reduction—a crucial step towards sustainable ...
Laura Legnani   +8 more
wiley   +1 more source

Investigating transthyretin variants H88R and I107V in amyloid priming: From destabilization to complete dissociation

open access: yesThe FEBS Journal, EarlyView.
Investigated mutations in transthyretin (TTR) disrupt the F87‐centered hydrophobic core that stabilizes its tetrameric structure. The mild I107V mutation weakens inter‐chain packing, while H88R fully abolishes tetramer formation, yielding a monomeric, aggregation‐prone form. Structural, biophysical, and computational analyses reveal that both mutations
István L. Bódy   +7 more
wiley   +1 more source

Quantum Information Entropy of Hyperbolic Potentials in Fractional Schrödinger Equation. [PDF]

open access: yesEntropy (Basel), 2022
Santana-Carrillo R   +5 more
europepmc   +1 more source

KU80 suppresses endonuclease G activity to preserve genomic integrity

open access: yesThe FEBS Journal, EarlyView.
Under normal conditions, EndoG remains restricted to mitochondria and the genome remains intact. When KU80 is absent, EndoG translocates into the nucleus, where it promotes DNA fragmentation and genomic instability. Thus, this work highlights the importance of KU80 in tightly controlling EndoG localization to preserve genome stability.
Jargalan Batsaikhan   +8 more
wiley   +1 more source

Genetic dissection reveals distinct contributions of the eS31 N‐terminal domain to translational accuracy in Saccharomyces cerevisiae

open access: yesThe FEBS Journal, EarlyView.
The eukaryote‐specific N‐terminal domain (NTD) of eS31 uses two distinct strategies to maintain translation fidelity. During elongation, a positively charged “hotspot” fine‐tunes the selection of incoming aa‐tRNA. During termination, the entire NTD acts as a structural scaffold to ensure the correct positioning of the release factor eRF1.
Qingxuan Gao   +3 more
wiley   +1 more source

Tyrosine residues at the substrate binding site in human NQO1 homodimer: Protein conformational dynamics and optimization of substrate binding geometry

open access: yesThe FEBS Journal, EarlyView.
Human NAD(P)H:quinone oxidoreductase 1 is a homodimeric flavoenzyme crucial for redox metabolism and linked to significant health issues. Point mutations at Tyr126 and Tyr128 demonstrate their essential roles in optimizing substrate binding geometry for catalysis, as well as in half‐site reactivity and conformational dynamics during the enzyme's ...
Maribel Rivero   +8 more
wiley   +1 more source

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