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Conformational dynamics and enzyme activity
scientific article published on 01 January 1998
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Europe PubMed Central
PubMed publication ID
9587660
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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9587660%20AND%20SRC:MED&resulttype=core&format=json
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11 November 2019
review article
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title
Conformational dynamics and enzyme activity
(English)
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Europe PubMed Central
PubMed publication ID
9587660
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11 November 2019
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J M Yon
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1
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PubMed publication ID
9587660
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11 November 2019
D Perahia
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2
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PubMed publication ID
9587660
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C Ghélis
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3
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9587660
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publication date
1 January 1998
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11 November 2019
published in
Biochimie
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PubMed publication ID
9587660
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volume
80
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PubMed publication ID
9587660
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11 November 2019
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1
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PubMed publication ID
9587660
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11 November 2019
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33-42
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11 November 2019
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Analysis of the low frequency normal modes of the T-state of aspartate transcarbamylase.
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Analysis of the low-frequency normal modes of the R state of aspartate transcarbamylase and a comparison with the T state modes
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An analysis of the conformational paths of citrate synthase
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The catalytic site of Escherichia coli aspartate transcarbamylase: interaction between histidine 134 and the carbonyl group of the substrate carbamyl phosphate
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Identifiers
DOI
10.1016/S0300-9084(98)80054-0
1 reference
stated in
Europe PubMed Central
PubMed publication ID
9587660
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9587660%20AND%20SRC:MED&resulttype=core&format=json
retrieved
11 November 2019
PubMed publication ID
9587660
1 reference
stated in
Europe PubMed Central
PubMed publication ID
9587660
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9587660%20AND%20SRC:MED&resulttype=core&format=json
retrieved
11 November 2019
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