De novo protein design by inversion of the AlphaFold structure prediction network
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The rate of formation of intramolecular interactions in unfolded proteins determines how fast conformational space can be explored during folding. Characterization of the dynamics of unfolded proteins is therefore essential for the understanding of the ear ...
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We report here the generation of mutants of the human O6-alkylguanine-DNA alkyltransferase (hAGT) for the efficient in vivo labeling of fusion proteins with synthetic reporter mols. Libraries of hAGT were displayed on phage, and mutants capable of efficien ...
An experimental system is described, permitting a detailed and systematic analysis of the factors governing self-assembly of amphipathic helices, e.g. to a four-helical bundle, a subject of major relevance for tertiary structure formation. protein folding ...
A review with 35 refs. Creating functional biol. mols. de novo requires a detailed understanding of the intimate relationship between primary sequence, folding mechanism, and packing topol., and remains up to now a most challenging goal in protein design a ...
We introduce a simplified protein model where the water degrees of freedom appear explicitly (although in an extremely simplified fashion). Using this model we are able to recover both the warm and the cold protein denaturation within a single framework, w ...
