A surprising simplicity to protein folding

By David Baker. Nature, 2000

721 citations recorded by the source corpus.

Subfields: Materials Chemistry, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/7d384fb0d620d4554d432308b7930aa3864c7d1a

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In Materials Chemistry

In Molecular Biology

Citations in the corpus

The structural basis of protein folding and its links with human disease. (2001, background): “within different structures (Plaxco et al. 1998; Chiti et al. 1999a; Baker 2000).”
Principles of protein folding, misfolding and aggregation. (2004, background): “Similar conclusions are emerging from computer simulations of the energy landscapes of proteins based on rather simple descriptions of the sequence-dependent properties of polypeptide chains[22].”
Coarse-grained models for proteins. (2005, background): “The success of this extremely simplified representation in reproducing several aspects of the thermodynamics and kinetics of folding is due to the fact that the folding process has generally evolved to satisfy the principle of minimal frustration [29].”
Protein folding and misfolding (2003, positive): “This evidence strongly supports the conclusion that there are relatively simple underlying principles by which the sequence of a protein encodes its structur”
Molecular Simulations of Cotranslational Protein Folding: Fragment Stabilities, Folding Cooperativity, and Trapping in the Ribosome (2006, neutral): “]. Significant insights into the process of protein refolding in vitro have been obtained through both experimental and theoretical techniques [”
TOUCHSTONE II: a new approach to ab initio protein structure prediction. (2003, background): “We also include biases to the expected contact order and contact number: E COCN ¼ w 14 ðN CO ÿ N 0 CO Þ 1 w 15 ðN CN ÿ N 0 CN Þ: (16) Here, N CO is the contact order of the given structure, defined as average sequence separation of residues in contact (Baker, 2000).”
Biomolecules under mechanical force (2010, background): “Recently, it was found that the folding of two-state proteins is surprisingly simple: their folding rates are just determined by the contact order [426].”