The in situ cyclization of proteins (INCYPRO) is a protein engineering technology that increases the durability of proteins and enzymes for biotechnological and biomedical applications.[1][2] For such applications, it is essential that the used proteins maintain their structural integrity.[3] This is, however, often challenged due to the conditions required for these applications which necessitates protein engineering to stabilize the protein structure.[4] The INCYPRO technology involves the attachment of molecular claps (crosslinks) to a protein, thereby reducing the tendency of the protein to unfold. The resulting INCYPRO-crosslinked proteins are more stable at elevated temperature and in presence of chemical denaturants.[5]
^Cite error: The named reference ”Pelay” was invoked but never defined (see the help page).
^Neubacher S, Saya JM, Amore A, Grossmann TN (February 2020). "In Situ Cyclization of Proteins (INCYPRO): Cross-Link Derivatization Modulates Protein Stability". The Journal of Organic Chemistry. 85 (3): 1476–1483. doi:10.1021/acs.joc.9b02490. PMC 7011175. PMID 31790232.
^Gligorijević V, Renfrew PD, Kosciolek T, Leman JK, Berenberg D, Vatanen T, et al. (May 2021). "Structure-based protein function prediction using graph convolutional networks". Nature Communications. 12 (1): 3168. Bibcode:2021NatCo..12.3168G. doi:10.1038/s41467-021-23303-9. PMC 8155034. PMID 34039967.
^Bornscheuer UT, Huisman GW, Kazlauskas RJ, Lutz S, Moore JC, Robins K (May 2012). "Engineering the third wave of biocatalysis". Nature. 485 (7397): 185–194. Bibcode:2012Natur.485..185B. doi:10.1038/nature11117. PMID 22575958. S2CID 4379415.
^Cite error: The named reference :1 was invoked but never defined (see the help page).
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