Using NMR spectroscopy to elucidate the role of molecular motions in enzyme function
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Conformational Rigidity and Protein Dynamics at Distinct Timescales Regulate PTP1B Activity and Allostery.Distinct Roles for Conformational Dynamics in Protein-Ligand Interactions.The Michaelis Complex of Arginine Kinase Samples the Transition State at a Frequency That Matches the Catalytic Rate.Probing the excited-state chemical shifts and exchange parameters by nitrogen-decoupled amide proton chemical exchange saturation transfer (HNdec-CEST).A gratuitous β-Lactamase inducer uncovers hidden active site dynamics of the Staphylococcus aureus BlaR1 sensor domain.Fast evaluation of protein dynamics from deficient 15N relaxation data.In Silico Studies of Small Molecule Interactions with Enzymes Reveal Aspects of Catalytic Function
P2860
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P2860
Using NMR spectroscopy to elucidate the role of molecular motions in enzyme function
description
2015 nî lūn-bûn
@nan
2015年の論文
@ja
2015年論文
@yue
2015年論文
@zh-hant
2015年論文
@zh-hk
2015年論文
@zh-mo
2015年論文
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2015年论文
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2015年论文
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2015年论文
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name
Using NMR spectroscopy to elucidate the role of molecular motions in enzyme function
@ast
Using NMR spectroscopy to elucidate the role of molecular motions in enzyme function
@en
type
label
Using NMR spectroscopy to elucidate the role of molecular motions in enzyme function
@ast
Using NMR spectroscopy to elucidate the role of molecular motions in enzyme function
@en
prefLabel
Using NMR spectroscopy to elucidate the role of molecular motions in enzyme function
@ast
Using NMR spectroscopy to elucidate the role of molecular motions in enzyme function
@en
P2860
P1476
Using NMR spectroscopy to elucidate the role of molecular motions in enzyme function
@en
P2093
George P Lisi
J Patrick Loria
P2860
P356
10.1016/J.PNMRS.2015.11.001
P577
2015-12-07T00:00:00Z