Biomedical Engineering Reference
In-Depth Information
70
6 60
55
5 45
4 35
30
2 20
15
1 5
0
70
6 60
55
5 45
4 35
30
2 20
15
1 5
0
70
6 60
55
5 45
4 35
30
2 20
15
1 5
0
0
100 200
Area/molecule (A° 2 )
300
400
0
100 200
Area/molecule (A° 2 )
300
400
0
100 200
Area/molecule (A° 2 )
300
400
A(I)
A(II)
A(III)
70
6 60
55
5 45
4 35
30
2 20
15
1 5
0
50
45
40
35
30
25
20
15
10
5
0
50
45
40
35
30
25
20
15
10
5
0
0
100 200
Area/molecule (A° 2 )
300
400
0
100 200
Area/molecule (A° 2 )
300
400
0
100 200
Area/molecule (A° 2 )
300
400
A(IV)
A(V)
A(VI)
2
0
50
45
40
35
30
25
20
15
10
5
0
200
220
240
260
280
-2
-4
-6
-8
-10
0
100 200
Area/molecule (A° 2 )
300
400
-12
Wave length (nm)
A(VII)
A
B
C
D
E
B
Figure 20.3. Surface pressure-area ( π -A) isotherm (A) : egg-Phosphatidylcholine (I), Choles-
terol (II), Galactocerebroside (III), (PTC : Chol : GalC) (1 : 0.35 : 0.125) deposited over PC polymer
surface, OCMC-A (C), OCMC-AH (D)., OCMC-AHP (E). Structure of the Albumin molecule incor-
porated into lipid bilayer (B) . CD spectra of albumin in its native (A) and altered state (B),
incorporated into PC (C), OCMC-A (D), OCMC-AHP (E).
albumin showed similar phase differences indicating the rearrangement of the
macromolecules. The CD spectra indicate that the secondary structure of the
native albumin is altered during the phase inversion. This altered structure is
retained irrespective of the lipid composition in all the protein lipid mixtures
(Figure 20.3 B).
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