Zobrazeno 1 - 10
of 48
pro vyhledávání: '"Joshua L. Price"'
Autor:
Jacob A. Stern, Tyler J. Free, Kimberlee L. Stern, Spencer Gardiner, Nicholas A. Dalley, Bradley C. Bundy, Joshua L. Price, David Wingate, Dennis Della Corte
Publikováno v:
Scientific Reports, Vol 13, Iss 1, Pp 1-8 (2023)
Abstract Various approaches have used neural networks as probabilistic models for the design of protein sequences. These "inverse folding" models employ different objective functions, which come with trade-offs that have not been assessed in detail b
Externí odkaz:
https://doaj.org/article/bfdd2c95245d460e8f802e7b5da5c735
Publikováno v:
Journal of Substance Use. 28:259-265
Autor:
Kimberlee L. Stern, Nicholas A. Dalley, Nathan T. McMurray, Wendy M. Billings, Taylor J. Loftus, Zachary B. Jones, Jacob R. Hadfield, Joshua L. Price
Publikováno v:
Biochemistry
Coiled coils are among the most abundant tertiary and quaternary structures found in proteins. A growing body of evidence suggests that long-range synergistic interactions among solvent-exposed residues can contribute substantially to coiled-coil con
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.
Autor:
Jacob A. Stern, Tyler J. Free, Kimberlee L. Stern, Spencer Gardiner, Nicholas A. Dalley, Bradley C. Bundy, Joshua L. Price, David Wingate, Dennis Della Corte
Several recently introduced approaches use neural networks as probabilistic models for protein sequence design. These models use various objective functions and optimization schemes. The choice of objective function and optimization scheme comes with
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::cd814bebad2bd73744ea6accb610bfbf
https://doi.org/10.1101/2022.12.28.521825
https://doi.org/10.1101/2022.12.28.521825
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
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
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
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