Protein Dynamism and Evolvability

By Nobuhiko Tokuriki, Dan S. Tawfik. Science, 2009

884 citations recorded by the source corpus.

Subfields: Materials Chemistry, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/26832df184159f04d773a7e5b6f94b80eabb1fc8

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In Materials Chemistry

In Molecular Biology

Citations in the corpus

Consensus protein design (2016, background): “Through the evolution of specialist function, many proteins now exist on a knife-edge of stability and function (Shoichet et al., 1995; Tokuriki et al., 2008; Tokuriki and Tawfik, 2009a, 2009b); for this reason, stabilising residues tend to be conserved.”
Enzyme promiscuity: a mechanistic and evolutionary perspective. (2010, background): “Adapted from Reference 69. same active-site The very same active site can therefore offer several different modes of interactions, and some of these might be utilized by promiscuous most of the describes cases analyzed by kinetics and site-directed mutagenesis.”
Stability effects of mutations and protein evolvability. (2009, background): “com progenitors, such a magnificent variety of proteins with different structures and functions had diverged (for further discussion of these issues see Reference [65]).”
Estimating conformational heterogeneity of tryptophan synthase with a template‐based Alphafold2 approach (2022, background): “…ensembles of pre-existing conformations in thermal equilibrium with the so-called native state are the basis for proteins' evolutionary adaptability 1 – 5 and provide an explanation for the observed divergency originated from a few common ancestors, 6 as well as their versatility as shown by the…”
Structured states of disordered proteins from genomic sequences (2016, neutral): “…gene regulation, signaling, and molecular transport, spurring growing interest in so-called disordered and low-complexity sequences (Bah et al., 2015; Ferreon et al., 2013; Motlagh et al., 2014; Tokuriki and Tawfik, 2009; Uversky and Dunker, 2010; Wells et al., 2008; Wright and Dyson, 2015).”
Exploring protein fitness landscapes by directed evolution (2009, neutral): “This is perhaps not surprising when we remember that a protein often undergoes conformational changes during function and exists as a dynamic ensemble of conformers that are only slightly more stable than their unfolded and non-functional states and that might themselves be functionally divers”
The Statistical Trends of Protein Evolution: A Lesson from AlphaFold Database (2022, neutral): “…disorder proteins (or regions) exhibit high dynamical plasticity, as shown in previous research (Meier and Özbek 2007; Tokuriki et al. 2008; Tokuriki and Tawfik 2009; Marsh and Teichmann 2014), but they may also exhibit high evolvability (towards more specialized function and towards new…”
The role of dynamic conformational ensembles in biomolecular recognition (2009, background): “, thus protein conformational diversity and functional promiscuity are closely connected and are a potential means of molecular evolutio”