Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Michael G. Souffrant"'
Publikováno v:
ACS Catalysis. 10:1810-1820
Allosteric regulations of the catalytic activity of enzymes in cellular processes remain poorly understood. Here, we advance the understanding of these critical processes by providing insights into...
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f34c564a10ba9f03825f75c1552550c9
https://doi.org/10.1021/acscatal.9b04404
https://doi.org/10.1021/acscatal.9b04404
Autor:
Giovanni Gadda, Donald Hamelberg, Michael G. Souffrant, Andreas S. Bommarius, John M. Robbins
Publikováno v:
Biochemistry. 56:3800-3807
Flavins, including flavin adenine dinucleotide (FAD), are fundamental catalytic cofactors that are responsible for the redox functionality of a diverse set of proteins. Alternatively, modified flavin analogues are rarely found in nature as their inco
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f398fa74d2340b619ee644ea9486f3b9
https://doi.org/10.1021/acs.biochem.7b00335
https://doi.org/10.1021/acs.biochem.7b00335
Publikováno v:
Biochemistry. 56:2477-2487
Mobile loops located at the active site entrance in enzymes often participate in conformational changes required to shield the reaction from bulk solvent, to control the access of the substrate to the active site, and to position residues for substra
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6c3ce8b5a37430ee01797a38b23e89b9
https://doi.org/10.1021/acs.biochem.7b00098
https://doi.org/10.1021/acs.biochem.7b00098
Publikováno v:
Journal of Chemical Information and Modeling. 56:139-147
Structurally conserved water molecules are important for biomolecular stability, flexibility, and function. X-ray crystallographic studies of Pin1 have resolved a number of water molecules around the enzyme, including two highly conserved water molec
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::25cab37bca7b7e3b0d7f7a90a2f4e957
https://doi.org/10.1021/acs.jcim.5b00560
https://doi.org/10.1021/acs.jcim.5b00560
Publikováno v:
Biochimica et biophysica acta. 1850(10)
Background Peptidyl prolyl cis–trans isomerization of the protein backbone is involved in the regulation of many biological processes. Cis–trans isomerization is notoriously slow and is catalyzed by a family of cis–trans peptidyl prolyl isomera
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2ce4b3d79dff16be104187f68c00b5db
https://pubmed.ncbi.nlm.nih.gov/25585011
https://pubmed.ncbi.nlm.nih.gov/25585011