Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Emily M. Dykstra"'
Autor:
Vlad K. Kumirov, Emily M. Dykstra, Taylor N. Szyszka, Matthew H. J. Cordes, Branwen M. Hall, William J. Anderson
Publikováno v:
Protein Science. 27:1767-1779
New protein folds may evolve from existing folds through metamorphic evolution involving a dramatic switch in structure. To mimic pathways by which amino acid sequence changes could induce a change in fold, we designed two folded hybrids of Xfaso 1 a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::fd381190d8bfe089e69409c3b143fb2b
https://doi.org/10.1002/pro.3488
https://doi.org/10.1002/pro.3488
Autor:
Jennifer Katcher, Molly S. Bolger, Lisa F. Rezende, Michele Nadler, Susan D. Hester, Lisa K. Elfring, Emily M. Dykstra
Publikováno v:
CBE Life Sciences Education
Providing opportunities for science, technology, engineering, and mathematics undergraduates to engage in authentic scientific practices is likely to influence their view of science and may impact their decision to persist through graduation. Laborat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::04efd7c4c28ae3ebb5aa7823116bac8e
http://europepmc.org/articles/PMC6755888
http://europepmc.org/articles/PMC6755888
Autor:
Matthew S. Dubrava, William J. Anderson, Emily M. Dykstra, Vlad K. Kumirov, Matthew H. J. Cordes, Karen V. Eaton
Publikováno v:
Protein engineering, designselection : PEDS. 28(8)
To study the sequence determinants governing protein fold evolution, we generated hybrid sequences from two homologous proteins with 40% identity but different folds: Pfl 6 Cro, which has a mixed α + β structure, and Xfaso 1 Cro, which has an all
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7f3b7ceb927186e4023a24cffb19df96
https://pubmed.ncbi.nlm.nih.gov/25991865
https://pubmed.ncbi.nlm.nih.gov/25991865
Publikováno v:
Recercat. Dipósit de la Recerca de Catalunya
instname
Dipòsit Digital de Documents de la UAB
Universitat Autònoma de Barcelona
Recercat: Dipósit de la Recerca de Catalunya
Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
instname
Dipòsit Digital de Documents de la UAB
Universitat Autònoma de Barcelona
Recercat: Dipósit de la Recerca de Catalunya
Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
In solid-state 2H NMR of fluid lipid bilayers, quasielastic deformations at MHz frequencies are detected as a square-law dependence of the nuclear spin-lattice (R(1Z)) relaxation rates and order parameters (S(CD)). The signature square-law slope is f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::691c064dda98f0bb8ab7a650a05a2cda
https://pubmed.ncbi.nlm.nih.gov/12513460
https://pubmed.ncbi.nlm.nih.gov/12513460