A growing team of groundbreaking scientists around the world are now sharing their lab notebooks online
Biologists interested in the function or the 3D shape of a certain protein face the task of isolating billions of copies of that protein from cells (a process called “protein purification” which does not involve washing or holy water). The aim of protein purification is to start with cells that contain the protein of interest Read More …
About one quarter of the Eukaryotic genome encodes glycoproteins that are made in the Endoplasmic Reticulum (ER), and travel to special destinations such as the extracellular environment, the cell membrane or other organelles like the lysosomes. We can think of the ER as a nursery where baby glycoproteins quickly grow to attain their adult Read More …
Nature has evolved molecules called glycoproteins that are proteins carrying sugar chains (“glycans”). Glycans can make proteins more soluble, they can shield them from the environment, they can be used as calling cards to enable protein-protein recognition; in Eukaryotes, a glucose-on/glucose-off quality control system uses glycans to monitor glycoproteins folding. In general, glycans contribute to Read More …
The inter-domain conformational mobility of UGGT, the eukaryotic secretion glycoprotein folding checkpoint, is likely key to its ability of recognising and re-glucosylating a vast number of different misfolded glycoproteins, bearing N-linked glycan(s) at various different distances from the site(s) of misfold. Ongoing Molecular Dynamics simulations by Juan Blanco, Carlos Modenutti, and Marcelo Martí in Buenos Read More …
