Biology Reference
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Table 2. The Theoretical Properties of Estimated Epitopes Assumed to be
One-domain-long Epitopes a
Peptide
position
Sequence
P0 part
MW [Da]
pI
52-76
HYAKGQPYIDEVGTFKERIQWVGDP
P0_Ex
2934.26
5.48
180-199
ASKRGRQTPVLYAMLDHSRS
P0_Int
2273.60
10.90
1-13
IVVYTDREVHGAV
P0_Ex
1457.65
5.32
14-26
GSRVTLHCSFWSS
P0_Ex
1466.63
8.26
102-123
NPPDIVGKTSQVTLYVFEKVPT
P0_Ex
2432.80
6.07
155-172
LRRQAALQRRLSAMEKGK
P0_Int
2112.53
12.01
168-179
MEKGKLHKPGKD
P0_Int
1367.63
9.52
200-219
TKAVSEKKAKGLGESRKDKK
P0_Int
2188.56
10.12
a The difference between overall pI (isoelectric point) of P0_Int epitopes and P0_Ex epitopes (52-76)
is 5.48; the intracellular part (180-199) is 10.90. A very similar situation occurs for the short epitopes:
the pI of extracellular epitopes ranges between ranges between 5.32-8.26, for intracellular epitopes
it ranges between 5.52-12.01.
Table 3. The Theoretical Properties of Estimated Epitopes Assumed to be
Two-domain-long Epitopes a
Peptide
position
Sequence
P0 part
MW [Da]
pI
52-76
HYAKGQPYIDEVGTFKERIQWVGDP
P0_Ex
2934.26
5.48
180-199
ASKRGRQTPVLYAMLDHSRS
P0_Int
2273.60
10.90
1-26
IVVYTDREVHGAVGSRVTLHCSFWSS
P0_Ex
2906.27
6.91
155-179
LRRQAALQRRLSAMEKGKLHKPGKD
P0_Int
2888.43
11.58
a It is likely that two-domain epitopes are more specific for autoimmune reaction than one-domain
epitopes. Physical properties of the long epitopes are more similar to adequate well-known epitopes.
part: first, a single hydrophobic
-strand located in the middle between
hydrophilic domains oriented by its hydrophobic residues into the center of
subunit; second, two antiparallel
β
-helixes. Our
calculations have confirmed previously published data (Luo et al ., 2007) on
the structure of the P0_Int part; the subunit is modeled as two
β
-strands parallel to the two
α
β
-strands par-
allel to two
-strands is known as an autoim-
mune epitope of P0 protein (Westall, 2006), it should be on the outside
surface of this subunit. This orientation is possible if the model consists of
α
-helixes. Since one of the
β
 
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