Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Dallin S. Ashton"'
Autor:
Qiang Xiao, Zachary B. Jones, Samantha C. Hatfield, Dallin S. Ashton, Nicholas A. Dalley, Cody D. Dyer, Judah L. Evangelista, Joshua L. Price
Publikováno v:
RSC Chemical Biology. 3:1096-1104
Here we identify key criteria for designing PEG-stapled coiled coils with increased conformational and proteolytic stability.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::91a7fa455b0095e3cf77dee1e0e3c42f
https://doi.org/10.1039/d1cb00237f
https://doi.org/10.1039/d1cb00237f
Autor:
Seth O Earl, Steven R. E. Draper, Nicholas A Dalley, Joshua L. Price, Dallin S Ashton, Benjamin M Conover, Anthony J Carter, Zachary B. Jones
Publikováno v:
Biochemistry
Here we show that an NH-π interaction between a highly conserved Asn and a nearby Trp stabilizes the WW domain of the human protein Pin1. The strength of this NH-π interaction depends on the structure of the arene, with NH-π interactions involving
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e3dac9d4d7b3dbcc9e79d8224043362c
https://doi.org/10.1021/acs.biochem.1c00132
https://doi.org/10.1021/acs.biochem.1c00132
Publikováno v:
RSC Chemical Biology
We previously showed that long-range stapling of two Asn-linked O-allyl PEG oligomers via olefin metathesis substantially increases the conformational stability of the WW domain through an entropic effect. The impact of stapling was more favorable wh
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c7792d60d9c03c67f4f82cb67f6440cd
http://europepmc.org/articles/PMC8009319
http://europepmc.org/articles/PMC8009319
Autor:
Qiang, Xiao, Zachary B, Jones, Samantha C, Hatfield, Dallin S, Ashton, Nicholas A, Dalley, Cody D, Dyer, Judah L, Evangelista, Joshua L, Price
Publikováno v:
RSC chemical biology. 3(9)
Macrocyclization or stapling is one of the most well-known and generally applicable strategies for enhancing peptide/protein conformational stability and target binding affinity. However, there are limited structure- or sequence-based guidelines for
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::2546c92c7ea0d301d29ca70b62f06789
https://pubmed.ncbi.nlm.nih.gov/36128502
https://pubmed.ncbi.nlm.nih.gov/36128502
Autor:
Qiang Xiao, K.L. Stern, Dallin S Ashton, Steven R. E. Draper, Anthony J Carter, Joshua L. Price, Benjamin M Conover
Publikováno v:
J Org Chem
Many proteins have one or more surface-exposed patches of non-polar residues; our observations here suggest that PEGylation near such locations might be a useful strategy for increasing protein conformational stability. Specifically, we show that con
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bcbbe9df914b2fe0ed01d62d502b28b7
https://doi.org/10.1021/acs.joc.9b02615
https://doi.org/10.1021/acs.joc.9b02615