Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Duncan W. S. MacKenzie"'
Autor:
Duncan W. S. MacKenzie, Anna Schaefer, Julia Steckner, Christopher A. Leo, Dalia Naser, Efrosini Artikis, Aron Broom, Travis Ko, Purnank Shah, Mikaela Q. Ney, Elisa Tran, Martin T. J. Smith, Brian Fuglestad, A. Joshua Wand, Charles L. Brooks, Elizabeth M. Meiering
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 119(26)
Allostery is the phenomenon of coupling between distal binding sites in a protein. Such coupling is at the crux of protein function and regulation in a myriad of scenarios, yet determining the molecular mechanisms of coupling networks in proteins rem
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f10fd9ff87b67f2d00a12c2f70002d74
https://pubmed.ncbi.nlm.nih.gov/35737838
https://pubmed.ncbi.nlm.nih.gov/35737838
Publikováno v:
Protein Science : A Publication of the Protein Society
Isotropic chemical shifts measured by solution nuclear magnetic resonance (NMR) spectroscopy offer extensive insights into protein structure and dynamics. Temperature dependences add a valuable dimension; notably, the temperature dependences of amide
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bb69d8d80117a8af0e4697f3fd972e1d
https://doi.org/10.1002/pro.3785
https://doi.org/10.1002/pro.3785
Publikováno v:
Current opinion in structural biology. 38
Protein design is still a challenging undertaking, often requiring multiple attempts or iterations for success. Typically, the source of failure is unclear, and scoring metrics appear similar between successful and failed cases. Nevertheless, the use
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8222b8d4f3d218388f23be8cade38dd4
https://pubmed.ncbi.nlm.nih.gov/27270240
https://pubmed.ncbi.nlm.nih.gov/27270240
Publikováno v:
Protein Engineering Design and Selection. 24:213-217
The energetic networks that govern regulated switching processes in macromolecules are poorly understood at a molecular level. We illustrate a general methodology that uses thermodynamic cycles to measure the coupling energetics between specific grou
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a13a6529bec3abc6d40565ce0586c97f
https://doi.org/10.1093/protein/gzq099
https://doi.org/10.1093/protein/gzq099
Autor:
Elizabeth M. Meiering, Fernando Bralha, Dalit Shental-Bechor, Duncan W. S. MacKenzie, Aron Broom, Chris Go, Amir Marcovitz, Fadila Ghashut, Martin T. J. Smith, Yaakov Levy
We present an integrated experimental and computational study of the molecular mechanisms by which myristoylation affects protein folding and function, which has been little characterized to date. Myristoylation, the covalent linkage of a hydrophobic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6d848ee69011176d46915c8a2aa4ece5
https://europepmc.org/articles/PMC3497764/
https://europepmc.org/articles/PMC3497764/
