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Comment
. 2023 Apr;32(4):e4602.
doi: 10.1002/pro.4602.

Comment on "Intrinsic protein disorder uncouples affinity from binding specificity"

Kaare Teilum  1 , Johan G Olsen  1 , Birthe B Kragelund  1
Affiliations
Comment

Comment on "Intrinsic protein disorder uncouples affinity from binding specificity"

Kaare Teilum et al. Protein Sci. 2023 Apr.
No abstract available

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Figures

FIGURE 1
FIGURE 1
Density estimates of ΔG° of binding for IDP:ordered complexes (ID‐OR, red) and for complexes between two globular ordered proteins (OR‐OR, blue). The distributions in light colors are from the data compiled by Lazar et al. (2022), whereas the distributions in darker colors are from the data compiled by Teilum et al. (2015). The dashed vertical lines show the average of each distribution.
See this image and copyright information in PMC

Comment in

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. Pauwels K, Tompa P. Editorial: function and flexibility: friend or foe? Front Mol Biosci. 2016;3:31. - PMC - PubMed
    1. Teilum K, Olsen JG, Kragelund BB. Globular and disordered—the non‐identical twins in protein‐protein interactions. Front Mol Biosci. 2015;2:40. - PMC - PubMed
    1. Teilum K, Olsen JG, Kragelund BB. On the specificity of protein–protein interactions in the context of disorder. Biochem J. 2021;478:2035–50. - PMC - PubMed

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