Zobrazeno 1 - 3
of 3
pro vyhledávání: '"Jens M. Hemmingsen"'
Publikováno v:
Protein Science. 3:1927-1937
The Tyr corner is a conformation in which a tyrosine (residue "Y") near the beginning or end of an antiparallel beta-strand makes an H bond from its side-chain OH group to the backbone NH and/or CO of residue Y - 3, Y - 4, or Y - 5 in the nearby conn
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cc4aef895c0324de8fdd1f73716e49ef
https://doi.org/10.1002/pro.5560031104
https://doi.org/10.1002/pro.5560031104
Autor:
Jens M. Hemmingsen, Joseph J. Villafranca, Jeffrey B. Schineller, Adil M. Dhalla, William M. Atkins, Murtaza F. Alibhai, Kenneth J. Yost, Bin Li
Publikováno v:
Protein Science. 3:476-481
In order to understand the nature of ATP and L-glutamate binding to glutamine synthetase, and the involvement of Arg 339 and Arg 359 in catalysis, these amino acids were changed to cysteine via site-directed mutagenesis. Individual mutations (Arg-->C
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5657c0d3dcd225534b87fa03951bcb81
https://doi.org/10.1002/pro.5560030313
https://doi.org/10.1002/pro.5560030313
Publikováno v:
Protein Science. 2:800-813
Adenylylation of Tyr-397 of each subunit of Escherichia coli glutamine synthetase (GS) down-regulates enzymatic activity in vivo. The overall structure of the enzyme consists of 12 subunits arranged as two hexamers, face to face. Research reported in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3386792dfc176f2b241979bd0305473c
https://doi.org/10.1002/pro.5560020510
https://doi.org/10.1002/pro.5560020510