Zobrazeno 1 - 10
of 193
pro vyhledávání: '"Howard K. Schachman"'
Publikováno v:
Journal of the American Chemical Society. 131:16534-16543
A number of complementary approaches for the assignment of Ile, Leu, and Val methyl groups in Methyl-TROSY spectra of supra-molecular protein complexes are presented and compared. This includes the transfer of assignments from smaller fragments to th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3692f309cc41d99b989ebe3d9cd0bc3c
https://doi.org/10.1021/ja906978r
https://doi.org/10.1021/ja906978r
Publikováno v:
Proceedings of the National Academy of Sciences. 104:8815-8820
The 306-kDa aspartate transcarbamoylase is a well studied regulatory enzyme, and it has emerged as a paradigm for understanding allostery and cooperative binding processes. Although there is a consensus that the cooperative binding of active site lig
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cae72fd33590c22d92193784b832a27a
https://doi.org/10.1073/pnas.0703347104
https://doi.org/10.1073/pnas.0703347104
Autor:
Howard K. Schachman
Publikováno v:
Journal of Biological Chemistry. 281:6889-6903
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::96e5b287297979f5a2fd5856ec6bb5f2
https://doi.org/10.1074/jbc.x600002200
https://doi.org/10.1074/jbc.x600002200
Autor:
Howard K. Schachman
Publikováno v:
Biophysical Chemistry. 108:9-16
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::23cc77a3c1314ed52591d654a96847e9
https://doi.org/10.1016/j.bpc.2003.10.005
https://doi.org/10.1016/j.bpc.2003.10.005
Autor:
N.N. Kalnine, Howard K. Schachman
Publikováno v:
Biophysical Chemistry. :133-144
Urea gradient gel electrophoresis combined with quantitative image processing of stained gels was used to analyze the dissociation and unfolding of the catalytic subunit of aspartate transcarbamoylase. The subunit, composed of three identical polypep
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f3fe8cd483bb2fa847710635dfba9270
https://doi.org/10.1016/s0301-4622(02)00154-0
https://doi.org/10.1016/s0301-4622(02)00154-0
Autor:
Howard K. Schachman, Lauren B. Murata
Publikováno v:
Protein Science. 5:719-728
Each catalytic (c) polypeptide chain of Escherichia coli aspartate transcarbamoylase (ATCase) is composed of two globular domains connected by two interdomain helices. Helix 12, near the C-terminus, extends from the second domain back through the fir
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0f49fedf51360e27bda058d58bd06213
https://doi.org/10.1002/pro.5560050417
https://doi.org/10.1002/pro.5560050417
Autor:
Lauren B. Murata, Howard K. Schachman
Publikováno v:
Protein Science. 5:709-718
Predictions of tertiary structures of proteins from their amino acid sequences are facilitated greatly when the structures of homologous proteins are known. On this basis, structural features of Escherichia coli ornithine transcarbamoylase (OTCase) w
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a098c51876a843a5c2ea7ce7f9fc4f42
https://doi.org/10.1002/pro.5560050416
https://doi.org/10.1002/pro.5560050416
Publikováno v:
Protein Science. 3:967-974
Interaction between a 70-amino acid and zinc-binding polypeptide from the regulatory chain and the catalytic (C) trimer of aspartate transcarbamoylase (ATCase) leads to dramatic changes in enzyme activity and affinity for active site ligands. The hyp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1ada1daba508272c61a90d7746f1a764
https://doi.org/10.1002/pro.5560030612
https://doi.org/10.1002/pro.5560030612
Autor:
Ying R. Yang, Howard K. Schachman
Publikováno v:
Proceedings of the National Academy of Sciences. 90:11980-11984
Based on the demonstration that active enzyme is formed in vitro and in vivo from polypeptide fragments of the catalytic chains of aspartate transcarbamoylase (ATCase; EC 2.1.3.2) and the evidence that NH2 and COOH termini of wild-type chains are in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::100f8e50161565a6547083baa31f4d29
https://doi.org/10.1073/pnas.90.24.11980
https://doi.org/10.1073/pnas.90.24.11980
Autor:
Ying R. Yang, Howard K. Schachman
Publikováno v:
Protein Science. 2:1013-1023
Despite the complexity of Escherichia coli aspartate transcarbamoylase (ATCase), composed of 12 polypeptide chains organized as two catalytic (C) trimers and three regulatory (R) dimers, it is possible to form active stable enzyme in vivo even with f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::16c0f74a62f0169b0e0d6305aee8e636
https://doi.org/10.1002/pro.5560020614
https://doi.org/10.1002/pro.5560020614