Designing a 20-residue protein

By J. Neidigh, R. Fesinmeyer, N. Andersen. Nature Structural Biology, 2002

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Detection of Functional Modes in Protein Dynamics (2009, methodology): “(PDB code 1L2Y [29]) was used as initial structure for the simulations of”
A de novo redesign of the WW domain (2003, background): “Andersen and co-workers prepared a 20-residue polypeptide capable of folding into a stable “Trp-cage” motif (Neidigh et al. 2002).”
Developing a molecular dynamics force field for both folded and disordered protein states (2018, background): “The a99SB-disp melting curves for villin, Trp-cage, and GTT, proteins that were not part of the training set, were also in much better agreement with experiment than the a99SB-ILDN/TIP4P-D melting curves, which showed no folded populations at any temperature for these proteins.”