Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Annette M. Bodenheimer"'
Publikováno v:
Carbohydrate Research. 448:200-204
Sensitivity to hydrogen/deuterium and lack of observable radiation damage makes cold neutrons an ideal probe the structural studies of proteins with highly photosensitive groups such as the copper center of lytic polysaccharide monooxygenases (LPMOs)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e06922c28547775c6005cd871439d159
https://doi.org/10.1016/j.carres.2017.03.001
https://doi.org/10.1016/j.carres.2017.03.001
Publikováno v:
Archives of Biochemistry and Biophysics. 602:48-60
Neutron protein crystallography is a powerful tool for investigating protein chemistry because it directly locates hydrogen atom positions in a protein structure. The visibility of hydrogen and deuterium atoms arises from the strong interaction of ne
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cd68ea6f200e185763f8e44824bbff97
https://doi.org/10.1016/j.abb.2015.11.033
https://doi.org/10.1016/j.abb.2015.11.033
Autor:
Christopher B. Stanley, Shuo Qian, William B. O'Dell, Flora Meilleur, Ryan C. Oliver, Annette M. Bodenheimer
Publikováno v:
Biochimica et biophysica acta. General subjects. 1862(4)
Background Cellobiose dehydrogenases have gained interest due to their potential applications in sectors from biofuel production to biomedical devices. The CDHIIA variant is comprised of a cytochrome domain (CYT), a dehydrogenase domain (DH), and a c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1e3c9b4e194b21c9fe6b4c3b19b60e3e
https://pubmed.ncbi.nlm.nih.gov/29374564
https://pubmed.ncbi.nlm.nih.gov/29374564
Autor:
Annette M. Bodenheimer, Flora Meilleur
Publikováno v:
FEBS letters. 590(23)
Trichoderma reesei Cel7A efficiently hydrolyses cellulose. We report here the crystallographic structures of the wild-type TrCel7A catalytic domain (CD) in an open state and, for the first time, in a closed state. Molecular dynamics (MD) simulations
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4bf890c147f77f6f89b22b1509cc32fe
https://pubmed.ncbi.nlm.nih.gov/27943301
https://pubmed.ncbi.nlm.nih.gov/27943301
Autor:
Annette M. Bodenheimer, Paul Swartz, Barbara R. Evans, Junhong He, Dean A. A. Myles, Matthew J. Cuneo, Flora Meilleur, Hugh O'Neill
Publikováno v:
Acta crystallographica. Section F, Structural biology communications. 70(Pt 6)
Cel7A (previously known as cellobiohydrolase I) fromHypocrea jecorinawas crystallized in two crystalline forms, neither of which have been previously reported. Both forms co-crystallize under the same crystallization conditions. The first crystal for
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::338222664441737b4e2f73c62488c5db
https://pubmed.ncbi.nlm.nih.gov/24915091
https://pubmed.ncbi.nlm.nih.gov/24915091
Crystal structures of wild-type Trichoderma reesei Cel7A catalytic domain in open and closed states.
Publikováno v:
FEBS Letters; Dec2016, Vol. 590 Issue 23, p4429-4438, 10p
Autor:
Bodenheimer, Annette M., Cuneo, Matthew J., Swartz, Paul D., He, Junhong, O'Neill, Hugh M., Myles, Dean A. A., Evans, Barbara R., Meilleur, Flora
Publikováno v:
Acta Crystallographica: Section F, Structural Biology Communications; Jun2014, Vol. 70 Issue 6, p773-776, 4p