Entropy drives selective fluorine recognition in the fluoroacetyl-CoA thioesterase from Streptomyces cattleya [Biochemistry]

Amy M. Weeks, Ningkun Wang, Jeffrey G. Pelton, Michelle C. Y. Chang
National Academy of Sciences
Published 2018
Publication Date:
2018-03-07
Publisher:
National Academy of Sciences
Print ISSN:
0027-8424
Electronic ISSN:
1091-6490
Topics:
Biology
Medicine
Natural Sciences in General
Published by:
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autor Amy M. Weeks, Ningkun Wang, Jeffrey G. Pelton, Michelle C. Y. Chang
beschreibung Fluorinated small molecules play an important role in the design of bioactive compounds for a broad range of applications. As such, there is strong interest in developing a deeper understanding of how fluorine affects the interaction of these ligands with their targets. Given the small number of fluorinated metabolites identified...
citation_standardnr 6197391
datenlieferant ipn_articles
feed_id 113
feed_publisher National Academy of Sciences
feed_publisher_url http://www.nasonline.org/
insertion_date 2018-03-07
journaleissn 1091-6490
journalissn 0027-8424
publikationsjahr_anzeige 2018
publikationsjahr_facette 2018
publikationsjahr_intervall 7984:2015-2019
publikationsjahr_sort 2018
publisher National Academy of Sciences
quelle PNAS - Proceedings of the National Academy of Sciences
relation http://www.pnas.org/content/115/10/E2193.short?rss=1
search_space articles
shingle_author_1 Amy M. Weeks, Ningkun Wang, Jeffrey G. Pelton, Michelle C. Y. Chang
shingle_author_2 Amy M. Weeks, Ningkun Wang, Jeffrey G. Pelton, Michelle C. Y. Chang
shingle_author_3 Amy M. Weeks, Ningkun Wang, Jeffrey G. Pelton, Michelle C. Y. Chang
shingle_author_4 Amy M. Weeks, Ningkun Wang, Jeffrey G. Pelton, Michelle C. Y. Chang
shingle_catch_all_1 Entropy drives selective fluorine recognition in the fluoroacetyl-CoA thioesterase from Streptomyces cattleya [Biochemistry]
Fluorinated small molecules play an important role in the design of bioactive compounds for a broad range of applications. As such, there is strong interest in developing a deeper understanding of how fluorine affects the interaction of these ligands with their targets. Given the small number of fluorinated metabolites identified...
Amy M. Weeks, Ningkun Wang, Jeffrey G. Pelton, Michelle C. Y. Chang
National Academy of Sciences
0027-8424
00278424
1091-6490
10916490
shingle_catch_all_2 Entropy drives selective fluorine recognition in the fluoroacetyl-CoA thioesterase from Streptomyces cattleya [Biochemistry]
Fluorinated small molecules play an important role in the design of bioactive compounds for a broad range of applications. As such, there is strong interest in developing a deeper understanding of how fluorine affects the interaction of these ligands with their targets. Given the small number of fluorinated metabolites identified...
Amy M. Weeks, Ningkun Wang, Jeffrey G. Pelton, Michelle C. Y. Chang
National Academy of Sciences
0027-8424
00278424
1091-6490
10916490
shingle_catch_all_3 Entropy drives selective fluorine recognition in the fluoroacetyl-CoA thioesterase from Streptomyces cattleya [Biochemistry]
Fluorinated small molecules play an important role in the design of bioactive compounds for a broad range of applications. As such, there is strong interest in developing a deeper understanding of how fluorine affects the interaction of these ligands with their targets. Given the small number of fluorinated metabolites identified...
Amy M. Weeks, Ningkun Wang, Jeffrey G. Pelton, Michelle C. Y. Chang
National Academy of Sciences
0027-8424
00278424
1091-6490
10916490
shingle_catch_all_4 Entropy drives selective fluorine recognition in the fluoroacetyl-CoA thioesterase from Streptomyces cattleya [Biochemistry]
Fluorinated small molecules play an important role in the design of bioactive compounds for a broad range of applications. As such, there is strong interest in developing a deeper understanding of how fluorine affects the interaction of these ligands with their targets. Given the small number of fluorinated metabolites identified...
Amy M. Weeks, Ningkun Wang, Jeffrey G. Pelton, Michelle C. Y. Chang
National Academy of Sciences
0027-8424
00278424
1091-6490
10916490
shingle_title_1 Entropy drives selective fluorine recognition in the fluoroacetyl-CoA thioesterase from Streptomyces cattleya [Biochemistry]
shingle_title_2 Entropy drives selective fluorine recognition in the fluoroacetyl-CoA thioesterase from Streptomyces cattleya [Biochemistry]
shingle_title_3 Entropy drives selective fluorine recognition in the fluoroacetyl-CoA thioesterase from Streptomyces cattleya [Biochemistry]
shingle_title_4 Entropy drives selective fluorine recognition in the fluoroacetyl-CoA thioesterase from Streptomyces cattleya [Biochemistry]
timestamp 2025-06-30T23:33:21.373Z
titel Entropy drives selective fluorine recognition in the fluoroacetyl-CoA thioesterase from Streptomyces cattleya [Biochemistry]
titel_suche Entropy drives selective fluorine recognition in the fluoroacetyl-CoA thioesterase from Streptomyces cattleya [Biochemistry]
topic W
WW-YZ
TA-TD
uid ipn_articles_6197391