Chemistry Reference
In-Depth Information
O
NH
2
Na
2
AMP
Na
2
GMP
N
N
N
NH
O
O
P
N
N
Na
+
O
−
O
Na
+
O
−
P
O
N
NH
2
N
O
O
O
−
O
−
Na
+
Na
+
OH HO
OH
OH
O
NH
2
Na
2
CMP
Na
2
UMP
NH
N
O
O
P
N
N
O
O
Na
+
O
−
Na
+
O
−
O
O
P
O
O
O
−
O
−
Na
+
Na
+
OH
OH
OH
OH
NH
2
O
N
N
HPA
P
N
O
N
O
H
3
C
OH
O
NH
2
O
OH
OH
N
O
N
CH
3
H
O
P
O
N
O
N
O
O
HO
CH
3
O
POPA
OH
OH
Figure 8.20
Mononucleotides disodium salts and nucleolipids (Murgia et al., 2009).
to explore the impact of the protein confi nement on its stability, unfolding
behavior, and morphology with severe external conditions, low pH, and higher
temperatures (up to 70°C).
The investigators focused on solubilizing insulin in GMO-decane-water,
GMO- decane - glycerol - water,
and
GMO - PC - decane - glycerol - water
mix-
tures and compared them to bulk solution (water).
The incorporation of insulin within the water and especially in the glycerol-
water cylinders compels the protein to be assembled in a restricted, confi ned
confi guration compared to its rearrangement in solution. The phenomenon of
a greater degree of compactness of the tertiary fold of insulin in the presence
of glycerol is known and here is overstressed upon its incorporation within the
water - and glycerol - fi lled cylinders, which limits its free volume. The ability to
obtain more confi ned protein structure, suggesting a more compact confi gura-
tion of solvated dimeric insulin, is expected to be mirrored by an enhancement
of the protein stability.
Search WWH ::
Custom Search