The following solvent accessibility information was derived from the information in Table 2 of reference [1]. The data for this table was calculated from data taken from 55 proteins in the Brookhaven data base, coming from 9 molecular families: globi ns, immunoglobins, cytochromes c, serine proteases, subtilisins, calcium binding proteins, acid proteases, toxins and virus capsid proteins.

NOTE: These two conditions ARE NOT equivalent!

The only clear trend in this table is that some residues, such as R and K, locate themselves so that they have access to the solvent. The so-called hydrophobic residues, such as L and F, show no clear trend: they are found near the solvent as often as they are found buried.

SEA = Solvent Exposed Area

Amino acid	SEA > 30 Å2	SEA < 10 Å2	30 > SEA > 10 Å2
S	0.70	0.20	0.10
T	0.71	0.16	0.13
A	0.48	0.35	0.17
G	0.51	0.36	0.13
P	0.78	0.13	0.09
C	0.32	0.54	0.14
D	0.81	0.09	0.10
E	0.93	0.04	0.03
Q	0.81	0.10	0.09
N	0.82	0.10	0.08
L	0.41	0.49	0.10
I	0.39	0.47	0.14
V	0.40	0.50	0.10
M	0.44	0.20	0.36
F	0.42	0.42	0.16
Y	0.67	0.20	0.13
W	0.49	0.44	0.07
K	0.93	0.02	0.05
R	0.84	0.05	0.11
H	0.66	0.19	0.15

Figure 1. The numbers indicate the probability that a particular residue will be positioned in real proteins so that its solvent exposed area meets the particular criterion in the column's title.