Thermodynamic analysis of substrate induced domain closure of 3-phosphoglycerate kinase.
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A spring-loaded release mechanism regulates domain movement and catalysis in phosphoglycerate kinaseConformational dynamics in phosphoglycerate kinase, an open and shut case?Nucleotide promiscuity of 3-phosphoglycerate kinase is in focus: implications for the design of better anti-HIV analoguesFunctional domain motions in proteins on the ~1-100 ns timescale: comparison of neutron spin-echo spectroscopy of phosphoglycerate kinase with molecular-dynamics simulation.Survey of the year 2009: applications of isothermal titration calorimetry.Modeling of solvent flow effects in enzyme catalysis under physiological conditions.
P2860
Thermodynamic analysis of substrate induced domain closure of 3-phosphoglycerate kinase.
description
2009 nî lūn-bûn
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2009年の論文
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2009年学术文章
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2009年学术文章
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name
Thermodynamic analysis of substrate induced domain closure of 3-phosphoglycerate kinase.
@en
Thermodynamic analysis of substrate induced domain closure of 3-phosphoglycerate kinase.
@nl
type
label
Thermodynamic analysis of substrate induced domain closure of 3-phosphoglycerate kinase.
@en
Thermodynamic analysis of substrate induced domain closure of 3-phosphoglycerate kinase.
@nl
prefLabel
Thermodynamic analysis of substrate induced domain closure of 3-phosphoglycerate kinase.
@en
Thermodynamic analysis of substrate induced domain closure of 3-phosphoglycerate kinase.
@nl
P2093
P2860
P1433
P1476
Thermodynamic analysis of substrate induced domain closure of 3-phosphoglycerate kinase.
@en
P2093
Andrea Varga
Beáta Flachner
Ferenc Vonderviszt
Judit Szabó
Péter Závodszky
Zoltán Gugolya
P2860
P304
P356
10.1016/J.FEBSLET.2009.10.048
P407
P577
2009-10-23T00:00:00Z