Intrinsically Disordered Protein: Difference between revisions
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Led by the assumption that “since amino acid sequence determines 3-D structure, amino acid sequence should also determine lack of 3-D structure” <ref name='Dunker2001'>PMID: 11533628</ref> specific sequence features shared by IUPs have been evaluated and algorithms for their identification formulated. | Led by the assumption that “since amino acid sequence determines 3-D structure, amino acid sequence should also determine lack of 3-D structure” <ref name='Dunker2001'>PMID: 11533628</ref> specific sequence features shared by IUPs have been evaluated and algorithms for their identification formulated. | ||
The low hydrophobicity and high net charge of natively unfolded proteins result in a difference in amino acid composition between them and | The low hydrophobicity and high [[net charge]] of natively unfolded proteins result in a difference in amino acid composition between them and natively folded proteins <ref>PMID: 11093259</ref>. | ||
Compared to sequences of ordered proteins, disordered protein sequences are substantially depleted in I, L, V, W, F, Y, and C, which were therefore designated as “order promoting” amino acids, and enriched in E, K, R, G, Q, S, P, and A, which have been designated as “disorder promoting”. The under representation of hydrophobic amino acids in a protein diminishes one of the basic thermodynamic forces known to be important for protein folding, namely, the hydrophobic interaction. Because a hydrophobic core does not form, such proteins have large hydrodynamic dimensions. | Compared to sequences of ordered proteins, disordered protein sequences are substantially depleted in I, L, V, W, F, Y, and C, which were therefore designated as “order promoting” amino acids, and enriched in E, K, R, G, Q, S, P, and A, which have been designated as “disorder promoting”. The under representation of hydrophobic amino acids in a protein diminishes one of the basic thermodynamic forces known to be important for protein folding, namely, the hydrophobic interaction. Because a hydrophobic core does not form, such proteins have large hydrodynamic dimensions. | ||
