Results 101 to 110 of about 12,579,753 (296)
FEBS Letters, EarlyView.Mycobacterial 3‐methylcrotonyl‐CoA carboxylase uses a mobile biotin‐carrying domain to shuttle a carboxyl group between two catalytic sites, enabling carboxylation of 3‐methylcrotonyl‐CoA during leucine breakdown. Cryo‐electron microscopy captures the carrier at both sites and reveals an inward loop movement that may prevent futile rebinding to the ...
Ajit Yadav +2 more
wiley +1 more source
Scientific ReportsIron storage proteins, e.g., vertebrate ferritin, and the ferritin-like bacterioferritin (Bfr) and bacterial ferritin (Ftn), are spherical, hollow proteins that catalyze the oxidation of Fe2+ at binuclear iron ferroxidase centers (FOC) and store the Fe3+
Huili Yao +9 more
doaj +1 more source
FEBS Letters, EarlyView.How do genomes gain new functional parts? In eukaryotes, which tend to evolve under weak selection, much of the genome is junk. Palazzo and Qiu borrow the logic of Markov chains to show how non‐functional DNA becomes functional through the appearance of intermediate states, which arise due to epistasis, buffering, and biochemical messiness, allowing ...
Alexander F. Palazzo, Yi Qiu
wiley +1 more source
Accurate and Automated Classification of
, 2003 PsiCSI is a highly accurate and automated method of assigning secondary structure from NMR data, which is a useful intermediate step in the determination of tertiary structures.
Protein Secondary Structure
core
The Shewanella oneidensis Fic enzyme SoFic targets the switch‐I region of EF‐Tu for AMPylation
FEBS Letters, EarlyView.Fic enzymes mediate diverse post‐translational modifications across all domains of life, including AMPylation. Prokaryotic EF‐Tu can be AMPylated and deAMPylated by the conserved Fic enzyme SoFic. Structural and biochemical approaches were used to characterize the effect of AMPylation on EF‐Tu, SoFic's enzymatic activities, and the enzyme‐target ...
Svenja Runge +6 more
wiley +1 more source
Results in ChemistryEmpirical structural methods have been instrumental in drug design, but they often fall short of capturing protein dynamics. To address this limitation, computer-aided drug design (CADD) is essential.
Mbalenhle Mfeka +5 more
doaj +1 more source
Chiral separation of chloroalkanes with the chromatographic column onboard Martian rovers
FEBS Letters, EarlyView.Computer image of the Rosalind Franklin Rover of ESA's ExoMars mission. ExoMars is scheduled to land on planet Mars in Oxia Planum in 2029. This area represents an interesting spot to look for biosignatures. Investigations of ExoMars include measurement on molecular chirality. We show that chiral chloroalkanes, that have been identified on Mars, can be
Asma Merzougui +4 more
wiley +1 more source
Prospecting the protein design landscape
FEBS Letters, EarlyView.This review outlines the current state of various protein design approaches. We discuss the current possibilities enabled by recently released tools, highlight future avenues to pursue in protein design, and underscore the crucial role of key databases and resources for successful protein design workflows.
Jakob R. Riccabona +4 more
wiley +1 more source
Single-molecule imaging of UvrA and UvrB recruitment to DNA lesions in living Escherichia coli
Nature Communications, 2016 Nucleotide excision repair is able to identify and remove a wide range of DNA helix distorting lesions from the genome. Here the authors use single molecule imaging of UvrA and UvrB molecules and suggest a two-step ‘scan and recruit’ model for UvrA ...
Mathew Stracy +6 more
doaj +1 more source
FEBS Letters, EarlyView.Synechocystis strains deficient in succinate dehydrogenase (SDH) secrete more succinate than the WT under dark anaerobic conditions, supporting that SDH then primarily acts as SDH, not as a fumarate reductase. L‐aspartate oxidase (Laspo) from Synechocystis is functional under anaerobic conditions, reducing fumarate to succinate.
Kateryna Kukil +3 more
wiley +1 more source