This paper describes recent advances of one-pot multi-segment condensation strategies based on kinetically controlled strategies and/or protecting group-removal strategies in chemical protein synthesis.
Water molecules play a key structure-organising role in the crystallisation of 15-crown-5 complexes of lithium and sodium TCNQ in the presence of excess TCNQ0.
During the total chemicals ynthesis of the watersoluble globular Haemophilus Influenzae DNAl igase (Hin-Lig), we observed the surprising phenomenon of as oluble peptide segment that failed to undergo native chemical ligation. Based on dynamic light scattering and transmission electron microscopye xperiments,w ed etermined that the peptide formed soluble colloidal particles in ah omogeneous solution containing 6 m guanidine hydrochloride.Conventional peptide performance-improving strategies,s uch as installation of at erminal/side-chain Arg tag or O-acyl isopeptide,f ailed to enable the reaction, presumably because of their inability to disrupt the formation of soluble colloidal particles.H owever, ar emovable backbone modification strategy recently developed for the synthesis of membrane proteins did disrupt the formation of the colloids,a nd the desired ligation of this soluble but unreactive system was eventually accomplished. This work demonstrates that an appropriate solution dispersion state,i na ddition to good peptide solubility,i sap rerequisite for successful peptide ligation.
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