Intrinsic motions along an enzymatic reaction trajectory

By K. Henzler-Wildman, V. Thai, M. Lei, M. Ott, M. Wolf-Watz, Timothy D Fenn, E. Pozharski, M. Wilson, G. Petsko, Martin Karplus and 2 more. Nature, 2007

844 citations recorded by the source corpus.

Subfields: Materials Chemistry, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/f2714fa8bef20c1614bc32eb91991b806a6822db

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In Materials Chemistry

In Molecular Biology

Citations in the corpus

Green function of correlated genes in a minimal mechanical model of protein evolution (2018, background): “Definition [7] is a direct link between epistasis and protein mechanics: The nonlinearity (‘curvature’) of the Green function measures the deviation of the mechanical response from additivity of the combined effect of isolated mutations at i and j, ∆Gi,j ≡ δGi,j−δGi−δGj .”
Integrating protein structural dynamics and evolutionary analysis with Bio3D (2014, background): “Notable examples include the dynamic rearrangements that facilitate many enzyme turnover events [3]; the force producing structural changes of motor proteins [4]; and the conformational and allosteric mechanisms that modulate protein associations in many signal transduction cascades [5,6].”
Binding of Small-Molecule Ligands to Proteins: “What You See” Is Not Always “What You Get” (2009, positive): “Multiple conformers are also seen in host-guest binding (Chang and Gilson, 2004; Chen et al., 2004) and can be critical for protein mechanisms such as enzyme catalytic motions (Eisenmesser et al., 2005; Arora and Brooks, 2007; Henzler-Wildman et al., 2007; Henzler-Wildman and Kern, 2007).”