. 2014 Jun 10;22(6):889–898. doi: 10.1016/j.str.2014.03.014

Table 2.

Solvent-Accessible Surface Area Changes on Unfolding

Protein	Native SASA (Å²)^a	Fully Unfolded SASA (Å²)^a	ΔSASA_N-I (Å²)^b	ΔSASA_I-D (Å²)^b	ΔSASA_N-D (Å²)^b
EGFP	9,919	31,849	7,050 ± 340	10,320 ± 440	17,370 ± 390
EGFP^G4Δ	9,366	31,953	5,430 ± 300	7,990 ± 370	13,420 ± 350

Calculated using the calc-surface program (http://helixweb.nih.gov/structbio/basic.html). Only residues K3–L231 were considered for SASA calculations. Unfolded state refers to fully unfolded peptide.

Calculated with the determined m values using BPPred (http://www-clarke.ch.cam.ac.uk/BPPred.php; Geierhaas et al., 2007).