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. 2001 Sep 25;98(20):11142–11147. doi: 10.1073/pnas.211424998

Table 2.

Relative hydrophobicities and conformational preferences of the differing amino acids of the ARAE motif in h/rCRF and the corresponding stretch in Svg

Equivalent residue
Rel. hydrophobicity
Secondary structure propensities
h/rCRF/Svg h/rCRF/Svg α-Helix (Pα) h/rCRF/Svg β-Structure (Pβ) h/rCRF/Svg Turn structure (Pt) h/rCRF/Svg
Ala22/Glu21 0.25/−0.62 1.41/1.59 0.72/0.52 0.82/1.01
Arg23/Lys22 −1.8/−1.1 1.21/1.23 0.84/0.69 0.90/1.07
Ala24/Gln23 0.25/−0.69 1.41/1.27 0.72/0.98 0.82/0.84

The relative hydrophobicities were taken from the consensus hydrophobicity scale of Eisenberg (24). Pα, Pβ, and Pt represent the normalized frequencies for each conformation (25).