The highly cooperative folding of small naturally occurring proteins is likely the result of natural selection.
By Alexander L Watters, Pritilekha Deka, Colin Corrent, David R. Callender, Gabriele Varani, Tobin R. Sosnick, David Baker. 2007
141 citations recorded by the source corpus.
Subfields: Materials Chemistry, Molecular Biology
How researchers see this paper
The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.
In Materials Chemistry
- Sergey Ovchinnikov
- David Baker
- David E. Kim
- Ivan V. Anishchenko
- Hetunandan Kamisetty
- Yang Zhang
- Christoffer H Norn
- Jinbo Xu
In Molecular Biology
- Sergey Ovchinnikov
- David Baker
- Hetunandan Kamisetty
- David E. Kim
- Ivan V. Anishchenko
- Yang Zhang
- Jinbo Xu
- David T. Jones
Citations in the corpus
- Learning generative models for protein fold families (2011, background): “For example, even successfully-designed proteins often exhibit non-natural behavior in terms of their thermal stability and folding pathways [37].”
- Protein sequence design by conformational landscape optimization (2021, background): “A limitation of all of these approaches, however, is that while they generate a sequence that is the lowest-energy sequence for the desired structure, they can result in rough energy landscapes that hamper folding (7, 8) and do not guarantee that the desired structure is the lowest-energy structure ”
- Stability effects of mutations and protein evolvability. (2009, background): “Thus, DG values lower than 3 kcal/mol might be required, in addition to the prevention of problematic folding intermediates [17].”
- Protein design with a comprehensive statistical energy function and boosted by experimental selection for foldability (2014, background): “In many cases, the designed proteins also lacked the rich conformational dynamics exhibited by their native counterparts 16 .”