Intrinsic dynamics of an enzyme underlies catalysis

By E. Eisenmesser, Ó. Millet, W. Labeikovsky, D. Korzhnev, M. Wolf-Watz, D. A. Bosco, J. Skalicky, Lewis E. Kay, Dorothee Kern. Nature, 2005

1,044 citations recorded by the source corpus.

Subfields: Epidemiology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/c4ede9585a748374441d2bf2391cf913a8d9ce71

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In Molecular Biology

Citations in the corpus

External electric field effects on chemical structure and reactivity (2020, background): “The biocatalytic function of many enzymes turns out to be significantly influenced by the electrostatic fields mediated by the charged functional groups scattered throughout the protein (as well as by the intrinsic dynamics).(17,18) The fine-tuning of the distribution of these point charges, in orde”
PROFbval: predict flexible and rigid residues in proteins (2006, background): “Such motions even happen in the enzyme cyclophilin A in its free form ( Eisenmesser, et al., 2005 ).”
p53 Proteoforms and Intrinsic Disorder: An Illustration of the Protein Structure–Function Continuum Concept (2016, background): “As a matter of fact, the biological functions of ordered proteins are known to be heavily dependent on the internal dynamics of enzymes, where individual amino acid residues, groups of amino acids, and even entire domains move relative to each other in a wide range of time scales, from femtoseconds ”
Chemical shift-based methods in NMR structure determination (2018, background): “High resolution modeling of sidechain conformations is of considerable interest towards understanding protein function with respect to enzyme catalysis [173], protein interactions modes [174] and folding [175].”
Patterns of coevolving amino acids unveil structural and dynamical domains (2017, background): “In particular, the secondary and higher-order structural organization of several proteins and enzymes are well suited to sustain collective conformational changes needed for function (3, 4, 14).”
Intrinsically Disordered Proteins and Their “Mysterious” (Meta)Physics (2019, background): “In fact, even in ordered proteins, functional dynamics involve movements of not only individual amino acid residues or groups of amino acids in an active site relative to each, but also displacements of entire domains, and these function-related movements that happen in a wide spread of time-scales,”
Green function of correlated genes in a minimal mechanical model of protein evolution (2018, background): “(C) The epistasis between two mutations, δHi and δHj , is equivalent to a series of multiple scattering paths [9].”