Zobrazeno 1 - 10
of 23
pro vyhledávání: '"Michelle E. McCully"'
Publikováno v:
Journal of Computational Chemistry. 43:197-205
The engineered three-helix bundle, UVF, is thermostabilized entropically due to heightened, native-state dynamics. However, it is unclear whether this thermostabilization strategy is observed in natural proteins from thermophiles. We performed all-at
Autor:
Matthew Gill, Michelle E. McCully
Publikováno v:
Protein Engineering, Design and Selection
Designing functional proteins that can withstand extreme heat is beneficial for industrial and protein therapeutic applications. Thus, elucidating the atomic-level determinants of thermostability is a major interest for rational protein design. To th
Autor:
Paulo Henrique Borges Ferreira, Ronaldo Junio de Oliveira, Gabriel Gouvêa Slade, Michelle E. McCully, Frederico Campos Freitas
Publikováno v:
J Chem Inf Model
Understanding which aspects contribute to the thermostability of proteins is a challenge that has persisted for decades, and it is of great relevance for protein engineering. Several types of interactions can influence the thermostability of a protei
Publikováno v:
Protein Eng Des Sel
Protein stability, dynamics and function are intricately linked. Accordingly, protein designers leverage dynamics in their designs and gain insight to their successes and failures by analyzing their proteins’ dynamics. Molecular dynamics (MD) simul
Publikováno v:
Biophysical Journal. 122:39a
Autor:
Gabriel Gouvêa Slade, Catrina Nguyen, Ronaldo Junio de Oliveira, Jennifer T. Young, Michelle E. McCully
Publikováno v:
Biophysical Journal
Thermostable proteins are advantageous in industrial applications, as pharmaceuticals or biosensors, and as templates for directed evolution. As protein-design methodologies improve, bioengineers are able to design proteins to perform a desired funct
Autor:
Qiang, Cui, Michelle E, McCully
Publikováno v:
Curr Opin Struct Biol
Publikováno v:
Biophysical Journal. 118:199a
Publikováno v:
Biophysical Journal. 118:198a
Publikováno v:
Biophysical Journal. 118:511a