A minimal sequence code for switching protein structure and function

By P. Alexander, Yanan He, Yihong Chen, J. Orban, P. Bryan. 2009

261 citations recorded by the source corpus.

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

Predicting multiple conformations via sequence clustering and AlphaFold2 (2023, positive): “Starting from two naturally occurring 56-amino-acid domains from the multidomain protein G, in which G A adopts a 3-α-helix and G B a 4b+a fold, variants had been engineered to switch between both folds 49–51 (Extended Data Fig.”
Intrinsic-Extrinsic Convolution and Pooling for Learning on 3D Protein Structures (2021, background): “As shown by Alexander et al. (2009), proteins with almost identical primary structure, i.e., only containing a few different amino acids, can fold into entirely different conformations.”
Mutational tipping points for switching protein folds and functions (2012, background): “, 2008), and GA95 (Alexander et al., 2009).”
Structured states of disordered proteins from genomic sequences (2016, unknown): “Bioinformatic algorithms that predict disorder are typically based on sequence bias that has in turn been learnt from experimental evidence from CD or NMR spectra (Alexander et al., 2009; Knowles et al., 2014; Mittag et al., 2008; Sambashivan et al., 2005; Tokuriki and Tawfik, 2009; Tompa, 2002; Uve”
An α-helix to β-barrel domain switch transforms the transcription factor RfaH into a translationfactor (2012, unknown): “Indeed, comparison of sequentially nearly identical, rationally designed proteins reveals that only a few amino acid residues encode the secondary structure (Alexander et al., 2009; Bryan and Orban, 2010).”