Abstract
Chemical synthesis of mirror‐image D‐version of the immunoglobulin‐like domain of TrkA (DlgCTrkA), a protein molecule needed for mirror‐image screening of D‐peptide ligands targeting TrkA, was found to be difficult due to the poor efficiency of intermediate synthesis and final protein folding. To solve this problem, the strategy of removable glycosylation modification was used and found to effectively improve the yield of peptide segment synthesis and ligation. Interestingly, it is important to note that temporary glycosylation at distinct sites of DlgCTrkA led to significant differences in the process of protein folding. More details are discussed in the article by Li et al. on pages 2316—2322.image
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
