Viscoelastic properties of dilute macromolecular solutions can provide information about molecular size and shape and an unambiguous test of flexibility. The Birnboim-Schrag multiple-lumped resonator will be used to study rigid or semiflexible rodlike molecules such as minifilaments of myosin and myosin rod, soluble collagen, xanthan polysaccharide, and schizophyllan polysaccharide. From the frequency dependence of the storage and loss shear moduli, the rotational relaxation time can be determined, as well as (if flexibility exists) the persistence length and micro-Young's modulus. Dynamic light scattering measurements may provide self-diffusion coefficients of macromolecules of various shapes in concentrated solutions and also in different environments such as concentrated solutions of another macromolecular species or gels. Mechanical properties of fibrin clots will be studied in small deformations and also in large deformations where changes in structure can be monitored by superposed small oscillating deformations during creep or stress relaxation. Birefringence will also be measured. These measurements provide information about the enhancement of structure at large strains, structural rearrangements and damage, and structural healing. Special attention will be given to clots from fibrinogen which retains its B peptides as well as that from which the Alpha appendages have been removed. Fibrin films made from such clots by removal of fluid to concentrate the system in one direction will be studied in stress relaxation. Gels, and films made from these gels, of other proteins such as gelatin and denatured bovine plasma albumin will be investigated by similar techniques, as well as, possibly, by high voltage electron microscopy and small-angle X-ray scattering.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM021652-12
Application #
3270622
Study Section
Biophysics and Biophysical Chemistry B Study Section (BBCB)
Project Start
1978-01-01
Project End
1988-12-31
Budget Start
1986-01-01
Budget End
1988-12-31
Support Year
12
Fiscal Year
1986
Total Cost
Indirect Cost
Name
University of Wisconsin Madison
Department
Type
Schools of Arts and Sciences
DUNS #
161202122
City
Madison
State
WI
Country
United States
Zip Code
53715
Miller, J W; Nestler, F H M; Schrag, J L (2004) Quantitative analysis of aggregation in dilute solutions of effectively rigid biomacromolecules via the combination of oscillatory flow birefringence and viscoelasticity measurements: example study of aggregation of bovine fibrinogen in aqueous glycerol, Biophys Chem 112:155-63
Muller, M F; Ferry, J D; Lin, J S (1989) Small-angle X-ray scattering studies of fibrin film: comparisons of fine and coarse films prepared with thrombin and ancrod. Biopolymers 28:1011-8
Shimizu, A; Schindlauer, G; Ferry, J D (1988) Interaction of the fibrinogen-binding tetrapeptide Gly-Pro-Arg-Pro with fine clots and oligomers of alpha-fibrin;comparisons with alpha beta-fibrin. Biopolymers 27:775-88
Shimizu, A; Ferry, J D (1988) Ligation of fibrinogen by factor XIIIa with dithiothreitol: mechanical properties of ligated fibrinogen gels. Biopolymers 27:703-13
Shimizu, A; Ferry, J D (1988) Clots of beta-fibrin. Viscoelastic properties, temperature dependence of elasticity, and interaction with fibrinogen-binding tetrapeptides. Biophys J 53:311-8
Nakatani, A I; Ferry, J D (1988) Thermally induced conformational changes in fibrin film. Thromb Res 52:361-7
Bale, M D; Ferry, J D (1988) Strain enhancement of elastic modulus in fine fibrin clots. Thromb Res 52:565-72
Schindlauer, G; Bale, M D; Ferry, J D (1986) Interaction of fibrinogen-binding tetrapeptides with fibrin oligomers and fine fibrin clots. Biopolymers 25:1315-36
Janmey, P A; Ferry, J D (1986) Gel formation by fibrin oligomers without addition of monomers. Biopolymers 25:1337-44
Bale, M D; Muller, M F; Ferry, J D (1985) Effects of fibrinogen-binding tetrapeptides on mechanical properties of fine fibrin clots. Proc Natl Acad Sci U S A 82:1410-3

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