Nativelike topology assembly of small proteins using predicted restraints in Monte Carlo folding simulations.

By Angel R. Ortiz, Andrzej Kolinski, J. Skolnick. 1998

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Citations in the corpus

Protein 3D Structure Computed from Evolutionary Sequence Variation (2011, background): “Previous work combined a small number of evolutionarily inferred residue contacts with other, structural, sources of information to successfully predict the structure of some smaller proteins, [16,17,18,19].”
Ab initio folding of proteins using restraints derived from evolutionary information (1999, background): “Overall, our CASP3 results are about what we qualitatively expected based on our benchmarks 4,16 and previous blind predictions.”
DESTINI: A deep-learning approach to contact-driven protein structure prediction (2019, background): “The idea was proposed decades ago 15,16 , and first implemented in the structure prediction algorithm MONSSTER 17 ; but at the time, its results were seriously limited due to the small library of evolutionarily related protein sequences that were available.”
MAMMOTH (Matching molecular models obtained from theory): An automated method for model comparison (2002, methodology): “…soon be possible to obtain functional annotations at genomic scale for new open reading frames following a sequence-structure-function paradigm (Thornton et al. 2000): First, structure prediction can be used to provide candidate folds for the query sequence (Ortiz et al. 1998a; Simons et al. 2001).”
Using inferred residue contacts to distinguish between correct and incorrect protein models (2008, methodology): “This correlation allows for confident rejection of incorrect structural models.”