The dynamic basis of structural order in proteins

We compare the sequences of folded and intrinsically disordered proteins (IDPs), using bioinformatic methods recently developed to study protein dynamic properties. We demonstrate that the two classes of sequences are organized in diametrically opposite ways with respect to long‐length‐scale dynamic...

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Bibliographic Details
Published in:Proteins, structure, function, and bioinformatics structure, function, and bioinformatics, 2022-05, Vol.90 (5), p.1115-1118
Main Authors: Konkankit, Chilaluck, Rackovsky, S.
Format: Article
Language:English
Subjects:
Amino acid composition
Amino Acids
Composition
Computational Biology
dynamic properties
intrinsically disordered proteins
Intrinsically Disordered Proteins - chemistry
Protein Conformation
Protein Folding
Proteins
Sequences
Statistical analysis
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Summary:We compare the sequences of folded and intrinsically disordered proteins (IDPs), using bioinformatic methods recently developed to study protein dynamic properties. We demonstrate that the two classes of sequences are organized in diametrically opposite ways with respect to long‐length‐scale dynamic properties. We further demonstrate a statistically significant difference between the amino acid compositions of folded and disordered proteins, which is expressed in dynamic properties. Our results indicate that the long‐length‐scale properties of sequences are critical in determining whether proteins are able to fold, and, more generally, that they are central to an understanding of protein physics. They further provide a physical basis for the empirically observed differences in amino acid composition between folded and IDPs.
ISSN:0887-3585
1097-0134
DOI:10.1002/prot.26296