Lily Lee’s Post

Protein folding - 5 The primary structure is held together by covalent peptide bonds. They are formed during the process of protein biosynthesis, where the amino acids lose one water molecule per reaction to attach to another amino acid. The secondary structure is determined by hydrogen bonds between the main-chain peptide groups. The tertiary structure is held by multiple types of bonds and forces, including hydrophobic interactions, hydrogen bonding, disulfide bridge, ionic bonding, as well as van der Waals forces. Among these forces, the non-specific hydrophobic interaction is the main force driving the folding of protein, while hydrogen bonds and disulfide bonds are responsible for maintaining the stable structure. The quaternary structure is also stabilized by the non-covalent interactions and disulfide bonds as in the tertiary structure, where more than one polypeptide is held together to form a single functional unit called multimer. Problem: Which of the following does not stabilize the tertiary structure of a protein? A) Hydrogen bonds B) Hydrophobic interactions C) Salt bridges D) Amide bonds E) Disulfide bonds Youtube video: https://lnkd.in/dZKw-cEe #nikolaysgeneticslessons

Current and emerging E3 ligase deconvolution approaches for degraders discovered from phenotypic screens or monovalent glue chemistry campaigns, highlighting future prospects for identifying more ligandable E3 ligases.

This new article is no on-line. If you have a research interest in ferroptosis this analytical methods is very interesting to better understand per oxidation of the cell membrane phase.

  This study measures photosynthesis in Capsicum annuum L. by principles of gas analysis and expression of enzyme ribulose-1,5-biphosphate carboxylase/oxygenase (rubisco), and demonstrates that a relationship exists between leaf temperature and photosynthesis. Observed relationship between leaf temperature and photosynthesis may be applicable to other C3 plants.   If you are interested in this topic you are welcome to read our article: https://lnkd.in/eddYkbMT

Effect of Surfactants on the in Vitro Germination of Pollen of Bitter-Gourd (Momordica Charantia L). https://lnkd.in/ghJQEa9h

Is purifying membrane proteins as challenging as thought? Various membrane proteins always have a specific orientation and are associated with different shapes on the phospholipid bilayer. It is relatively easier to strip peripheral and surface proteins from the membrane because they do not extend to the inner hydrophobic part and are bound by non-covalent interactions. However, purifying transmembrane and integral proteins with structures extending to the hydrophobic part of the membrane is challenging. This is due to the protein's structural apolarity when in contact with the hydrophobic part of the phospholipid bilayer. Consequently, the pre-purification step must also be highly efficient to ensure high protein recovery before chromatography. The incremental cost of cell lysis to recover hydrophobic proteins should also be considered.

Despite numerous optimizations in peptide synthesis, the formation of aspartimide remains a significant side reaction that needs to be addressed. An innovative approach that utilizes hydrazide as a carboxylic-acid-protecting group to reduce the formation of aspartimide. The aspartic acid hydrazide effectively suppresses the formation of aspartimide, even under microwave conditions, and is readily converted to native aspartic acid using CuSO4 in an aqueous medium. https://lnkd.in/g7CERf7Y

Enzyme Mastermixes ► https://loom.ly/meXs1uY Designed to minimize primer dimer artifacts and optimize Cq performance. Each mastermix contains dNTPs, Mg2+, salts, buffer, glycerol, and DNA polymerase.

Stability is an important characteristic of excipients for LNP delivery systems.Excipients interact with lipid components, increasing the stability of LNP.For example, polyethylene glycol (PEG) is one of the commonly used excipients, which can form a stable layer of polymer by covering the surface of LNP.This polymer layer helps to reduce protein and cell adsorption and provides additional stability, thereby prolonging the circulation life of LNP. https://lnkd.in/gjau-hSX #LNP #ChemicalMaterials

Can NaBH4 act as a reducing agent for esters? Check out the final chapter of my thesis, which explores the electrostatic templating abilities of short peptide nanotubes towards hydride-rich model cofactor NaBH4 for efficient ester reduction in water, published @Nature Communications (Nature Portfolio) Article Link: https://lnkd.in/gMZUz8Ya #Systemschemistry #Shortpeptides #Amyloid #Catalysis #Enzymemimics