HIGHLIGHTS
SUMMARY
Understanding how an IDP`s amino_acid sequence dictates the equilibrium and the dynamical properties of its conformational ensemble is an important step toward understanding the principles of function of this class of proteins. Typically, the mean hydrophobicity is lower and the mean net charge is higher in IDP sequences than in folded proteins, and they are impoverished in large amino_acids, preventing the folding of IDPs into unique stable structures with a hydrophobic core. In one study, a predictor based on the reduction the size of the sequence alphabet by assigning each amino_acid to just . . .
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