Physical Background of the Disordered Nature of “Mutual Synergetic Folding” Proteins
Abstract
:1. Introduction
2. Results
2.1. Sequence-Based Analysis
2.2. Structure-Based Analysis
3. Discussion
4. Materials and Methods
Supplementary Materials
Author Contributions
Funding
Conflicts of Interest
Abbreviations
IDPs | Intrinsically disordered proteins |
MFIB | Mutual Folding Induced by Binding database |
DIBS | Disordered Binding Site database |
ELMs | Short motifs of polypeptide chains |
MFHD | MFIB homodimeric dataset |
MSF | Mutual synergistic folding |
GLHD | Globular homodimeric dataset |
GLMD | Globular monomeric dataset |
PCA | Principal component analysis |
PDB | Protein data bank |
RSAMPs | Residues with solvent accessible main-chain patches |
SC/SCE | Stabilization centers/stabilization center elements |
SASA | Solvent accessible surface area |
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Magyar, C.; Mentes, A.; Fichó, E.; Cserző, M.; Simon, I. Physical Background of the Disordered Nature of “Mutual Synergetic Folding” Proteins. Int. J. Mol. Sci. 2018, 19, 3340. https://doi.org/10.3390/ijms19113340
Magyar C, Mentes A, Fichó E, Cserző M, Simon I. Physical Background of the Disordered Nature of “Mutual Synergetic Folding” Proteins. International Journal of Molecular Sciences. 2018; 19(11):3340. https://doi.org/10.3390/ijms19113340
Chicago/Turabian StyleMagyar, Csaba, Anikó Mentes, Erzsébet Fichó, Miklós Cserző, and István Simon. 2018. "Physical Background of the Disordered Nature of “Mutual Synergetic Folding” Proteins" International Journal of Molecular Sciences 19, no. 11: 3340. https://doi.org/10.3390/ijms19113340