Unraveling Photocatalytic Mechanism and Selectivity in PET‐RAFT Polymerization
نویسندگان
چکیده
منابع مشابه
Mechanism of selectivity in aquaporins and aquaglyceroporins.
Aquaporins and aquaglyceroporins form a family of pore proteins that facilitate the efficient and selective flux of small solutes across biological membranes. We studied the selectivity of aquaporin-1 (AQP1) and the bacterial glycerol facilitator, GlpF, for O(2), CO(2), NH(3), glycerol, urea, and water. Using molecular dynamics simulations, we calculated potentials of mean force for solute perm...
متن کاملMechanism of immunoglobulin A polymerization.
Employing mercaptoethylamine as a reducing agent, it was demonstrated by analytical ultracentrifugation and polyacrylamide gel electrophoresis that polymeric immunoglobulin A (IgA) was reduced to a 10 S dimer and 7 S monomer, and that dimer IgA was more resistant to reductive cleavage than the higher polymers. When dimer and monomer IgA were subjected to electrophoresis in polyacrylamide gels i...
متن کاملUnraveling the mechanism of electrospray ionization.
Electrospray ionization (ESI) generates intact gas-phase ions from analytes in solution for mass spectrometric investigations. ESI can proceed via different mechanisms. Low molecular weight analytes follow the ion evaporation model (IEM), whereas the charged residue model (CRM) applies to large globular species. A chain ejection model (CEM) has been proposed for disordered polymers.
متن کاملUnraveling the mechanism of protein N-glycosylation.
Asparagine-linked glycosylation is the most ubiquitous protein co-translational modification in the endoplasmic reticulum (ER). The enzyme that catalyzes this process is called oligosaccharyl transferase (OT). It catalyzes the transfer of an oligosaccharyl moiety (Glc3Man9GlcNAc2) from the dolichol-linked pyrophosphate donor to the side chain of Asn within a consensus sequence of Asn-X-Thr/Ser,...
متن کاملUnraveling the catalytic mechanism of nitrile hydratases.
To elucidate a detailed catalytic mechanism for nitrile hydratases (NHases), the pH and temperature dependence of the kinetic constants k(cat) and K(m) for the cobalt-type NHase from Pseudonocardia thermophila JCM 3095 (PtNHase) were examined. PtNHase was found to exhibit a bell-shaped curve for plots of relative activity versus pH at pH 3.2-11 and was found to display maximal activity between ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Advanced Theory and Simulations
سال: 2019
ISSN: 2513-0390,2513-0390
DOI: 10.1002/adts.201900038