277 papers
Biochemistry explores the intricate chemical processes that power life, bridging the gap between biology and chemistry to explain how molecules like proteins and DNA function within living cells. This field reveals the molecular machinery behind everything from metabolism to genetic inheritance, turning complex biological mysteries into understandable chemical interactions.
On Gist.Science, we bring you the freshest discoveries in this dynamic area directly from bioRxiv. Our team processes every new preprint uploaded to the server, transforming dense academic findings into both clear, plain-language overviews and detailed technical summaries. This dual approach ensures that whether you are a curious beginner or a seasoned researcher, you can grasp the significance of these breakthroughs immediately.
Below are the latest papers in biochemistry, complete with our curated summaries to help you navigate the cutting edge of molecular science.
This study elucidates the structure, biosynthesis, and bioactivity of nostolysamides, a novel class of acylated lanthipeptides from *Nostoc punctiforme*, revealing their unique ring topology, the non-essential role of acylation for their membrane-disrupting antibacterial and antifungal activities, and the broad substrate specificity of the acyltransferase NpuN.
This study demonstrates that red and near-infrared light (620–820 nm) activates mitochondrial large-conductance calcium-activated potassium channels in glioblastoma cells, likely via cytochrome c oxidase, suggesting a potential non-pharmacological approach for cytoprotection.
This study demonstrates that attenuated total reflectance Fourier transform infrared (ATR-FTIR) spectroscopy, combined with regression modeling, enables rapid, label-free, and non-destructive global quantification of DNA 5-methylcytosine and 5-hydroxymethylcytosine modifications, including in circulating tumor DNA samples.
This study identifies and characterizes thermolanthin, a novel class II lanthipeptide from the thermophilic bacterium *Thermoactinomyces* sp. DSM 45891, which features unique DL-(methyl)lanthionine ring structures deviating from typical stereoselectivity and exhibits antimicrobial activity against Gram-negative ESKAPE pathogens.
This study identifies TvAPT, a cyanobacterial adenine prenyltransferase with an enlarged binding pocket that enables the unprecedented N6-prenylation of adenine substrates using extended C10 and C15 prenyl donors, thereby expanding the chemical space for biomolecular engineering.
This study presents the first high-resolution cryo-EM structure of human ATAD2B, revealing its functional hexameric architecture and biochemical activity to provide mechanistic insights into its role as a dysregulated AAA+ ATPase in disease states.
This study elucidates the structure-interaction relationship between polymyxin lipopeptides and the human oligopeptide transporter hPepT2 through integrated computational and experimental approaches, identifying critical binding residues and demonstrating that specific analogues with reduced hPepT2 interaction retain antibacterial efficacy while significantly lowering nephrotoxicity.
This study demonstrates that the dynamic assembly and dissociation of the yeast mitochondrial MDH1-CIT1 metabolon are regulated by respiratory activity, mitochondrial matrix pH, and specific metabolite levels, serving as a key mechanism for TCA cycle adaptation to cellular metabolic demands.
This study reveals that two conserved acidic residues in GHKL ATPases cooperatively mediate early ATP hydrolysis, with one primarily positioning the nucleophilic water and the other acting as a general base, a mechanism whose disruption by disease-associated variants in human MutL homologs underscores its functional importance and evolutionary conservation.
This study reveals that negative DNA supercoiling dramatically accelerates Cas9 off-target cleavage and alters its cutting sites, demonstrating that DNA topology critically influences Cas9 specificity and necessitates topological considerations for safer gene editing.