Solvent accessibility of AA in known protein structures

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. Red entries are found on the surface of a proteins on > 70% of occurrences and blue entries are found inside of a protein of < 20% of occurrences.

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 Ň2 SEA < 10 Ň2 30 > SEA > 10 Ň2
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 columnís title.
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