  Conformational properties of intrinsically disordered proteins (IDPs) are
governed by a sequence-ensemble relationship. To differentiate the impact of
sequence-local versus sequence-nonlocal features of an IDP's charge pattern on
its conformational dimensions and its phase-separation propensity, the charge
"blockiness'' $\kappa$ and the nonlocality-weighted sequence charge decoration
(SCD) parameters are compared for their correlations with isolated-chain radii
of gyration ($R_{\rm g}$s) and upper critical solution temperatures (UCSTs) of
polyampholytes modeled by random phase approximation, field-theoretic
simulation, and coarse-grained molecular dynamics. SCD is superior to $\kappa$
in predicting $R_{\rm g}$ because SCD accounts for effects of contact order,
i.e., nonlocality, on dimensions of isolated chains. In contrast, $\kappa$ and
SCD are comparably good, though nonideal, predictors of UCST because
frequencies of interchain contacts in the multiple-chain condensed phase are
less sensitive to sequence positions than frequencies of intrachain contacts of
an isolated chain, as reflected by $\kappa$ correlating better with
condensed-phase interaction energy than SCD.
