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Comment
. 2023 Apr;32(4):e4601.
doi: 10.1002/pro.4601.

Reply to "Intrinsic protein disorder uncouples affinity from binding specificity"

Tamás Lázár  1   2 , Agnes Tantos  3 , Peter Tompa  1   2   3 , Eva Schad  3
Affiliations
Comment

Reply to "Intrinsic protein disorder uncouples affinity from binding specificity"

Tamás Lázár et al. Protein Sci. 2023 Apr.
No abstract available

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Figures

FIGURE 1
FIGURE 1
Interaction types of ID and globular complexes. (a) Percental distribution of interaction types (HYD: hydrophobic; HBridge: hydrogen bond; ION: ionic; OTHER: disulfide bridges, aromatic–aromatic, aromatic–sulfur, and cation–pi interactions) in strong and weak complexes (red: all ID complexes; dark red: strong; rose: weak ID complexes; blue: all globular complexes; dark blue: strong; light blue: weak globular complexes). Error bars represent mean ± SD. Original figure: fig. 5a in Lazar et al. (2022).
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Comment on

References

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    1. Lazar T, Tantos A, Tompa P, Schad E. Intrinsic protein disorder uncouples affinity from binding specificity. Protein Sci. 2022;31:e4455. - PMC - PubMed
    1. Liu Z, Huang Y. Advantages of proteins being disordered. Protein Sci. 2014;23:539–50. - PMC - PubMed

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