Enzyme Dynamics During Catalysis

By E. Eisenmesser, D. A. Bosco, M. Akke, Dorothee Kern. Science, 2002

658 citations recorded by the source corpus.

Subfields: Atomic and Molecular Physics, and Optics, Immunology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/262a67681b117dd56ee723388c1a0a81577fa9ae

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In Atomic and Molecular Physics, and Optics

In Immunology

In Molecular Biology

Citations in the corpus

Binding of Small-Molecule Ligands to Proteins: “What You See” Is Not Always “What You Get” (2009, neutral): “Several other studies also have provided evidence for multiple protein conformations (Eisenmesser et al., 2002; Gerstein et al., 1994; Min et al., 2005a, 2005b; Fragai et al., 2006).”
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).”
Dynamics of proteins in solution (2019, background): “In fact, slow (nanosecond–millisecond) collective dynamics along the backbone of proteins could be observed also by NMR (Eisenmesser et al., 2002; Wolf-Watz et al., 2004; Vögeli and Yao, 2009; Fenwick et al., 2016), usually at a residue level, although also the domain motion could be measured by…”
Methods in Enzymology: “Flexible backbone sampling methods to model and design protein alternative conformations” (2013, positive): “…either state (yellow/green) using backrub (right, cyan) but not fixed backbone (middle, magenta) sampling methods. the active site into the core of the protein and established a link between the rate of conformational exchange and the catalytic cycle of the enzyme (Eisenmesser et al., 2002, 2005).”
Sensitivity analysis practices: Strategies for model-based inference (2006, methodology): “In [85] SA is used to calibrate an over-parameterised model, where the amount of data is insufficient to estimate the whole set of model parameters (kinetic constants).”
Protein sectors: evolutionary units of three-dimensional structure (2009, background): “Indeed, a large body of experimental work now argues that amino acids contribute cooperatively but unequally in specifying protein structure and function (Agarwal et al., 2002; Benkovic and Hammes-Schiffer, 2003; Clackson and Wells, 1995; Datta et al., 2008; Eisenmesser et al., 2002; Fuentes et al.,”
Implications of protein flexibility for drug discovery (2003, background): “For instance, it has been shown that it is possible to correlate the motion of key catalytic residues with the frequency of transition-state formation and deca”
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 ”
Assessment of protein structure refinement in CASP9 (2011, background): “Flexibility is often crucial for a protein’s biological role [28, 29, 30].”
Evolutionarily conserved networks of residues mediate allosteric communication in proteins (2003, positive): “In addition, recent work has provided important clues that site-specific correlated motions in proteins are key determinants of functio”
Prolyl cis-trans isomerization as a molecular timer. (2007, background): “However, subsequent solution NMR dynamics studies of CypA in action on a four-residue peptide substrate were interpreted in support of a C-terminal rotation mechanis”