Direct observation in solution of a preexisting structural equilibrium for a mutant of the allosteric aspartate transcarbamoylase.
about
Allosteric communication occurs via networks of tertiary and quaternary motions in proteinsAn Allosteric Circuit in Caspase-1Crystallographic and Kinetic Evidence of Allostery in a Trypsin-like ProteaseSolution Structural Ensembles of Substrate-Free Cytochrome P450 camTrapping and structure determination of an intermediate in the allosteric transition of aspartate transcarbamoylaseStructure and mechanisms of Escherichia coli aspartate transcarbamoylaseTime Evolution of the Quaternary Structure of Escherichia coli Aspartate Transcarbamoylase upon Reaction with the Natural Substrates and a Slow, Tight-Binding InhibitorX-ray Scattering Studies of Protein Structural Dynamics.Ligand depletion in vivo modulates the dynamic range and cooperativity of signal transduction.Convergent transmission of RNAi guide-target mismatch information across Argonaute internal allosteric network.Allostery and cooperativity in Escherichia coli aspartate transcarbamoylaseIntrinsic dynamics of enzymes in the unbound state and relation to allosteric regulationSolution NMR Spectroscopy for the Study of Enzyme Allostery.Allostery: absence of a change in shape does not imply that allostery is not at play.Influence of the cosolute environment on IgG solution structure analyzed by small-angle X-ray scattering.Structural model of the R state of Escherichia coli aspartate transcarbamoylase with substrates bound.Frameworks for understanding long-range intra-protein communication.Global dynamics of proteins: bridging between structure and function.Protein functional landscapes, dynamics, allostery: a tortuous path towards a universal theoretical framework.Conformational selection or induced fit? 50 years of debate resolved.Dissecting enzyme regulation by multiple allosteric effectors: nucleotide regulation of aspartate transcarbamoylase.The core of allosteric motion in Thermus caldophilus L-lactate dehydrogenase
P2860
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P2860
Direct observation in solution of a preexisting structural equilibrium for a mutant of the allosteric aspartate transcarbamoylase.
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
2007年论文
@zh
2007年论文
@zh-cn
name
Direct observation in solution ...... c aspartate transcarbamoylase.
@ast
Direct observation in solution ...... c aspartate transcarbamoylase.
@en
type
label
Direct observation in solution ...... c aspartate transcarbamoylase.
@ast
Direct observation in solution ...... c aspartate transcarbamoylase.
@en
prefLabel
Direct observation in solution ...... c aspartate transcarbamoylase.
@ast
Direct observation in solution ...... c aspartate transcarbamoylase.
@en
P2093
P2860
P356
P1476
Direct observation in solution ...... c aspartate transcarbamoylase.
@en
P2093
Evan R Kantrowitz
Luc Fetler
Patrice Vachette
P2860
P304
P356
10.1073/PNAS.0607641104
P407
P577
2007-01-03T00:00:00Z