Interacting processes in protein coagulation

Proteins: Structure, Function and Genetics

Volumn 37, Issue 1, 1999, Pages 116-120

  San Biagio, P L ^a,c   Martorana, V ^a,c   Emanuele, A ^a,b   Vaiana, S M ^a,b   Manno, M ^a,b,c   Bulone, D ^a,c   Palma Vittorelli, M B ^a,b   Palma, M U ^a,b,c  

^a INFM   (Italy)

^b UNIVERSITY OF PALERMO   (Italy)

^c CNR   (Italy)

Author keywords

Amyloid deposits; BSA; Conformational changes; Intermolecular cross linking; Neurodegenerative diseases; Prions; Protein; Protein cross linking; Protein misfolding unfolding; Protein solvent interaction; Spinodal demixing

Indexed keywords

BOVINE SERUM ALBUMIN; POLYMER;

ALZHEIMER DISEASE; AMYLOIDOSIS; ARTICLE; CONFORMATIONAL TRANSITION; DEGENERATIVE DISEASE; PRION DISEASE; PRIORITY JOURNAL; PROTEIN CROSS LINKING; PROTEIN INTERACTION;

ALZHEIMER DISEASE; AMYLOIDOSIS; ANIMALS; CATTLE; CIRCULAR DICHROISM; ELASTICITY; HUMANS; NERVE TISSUE PROTEINS; PRION DISEASES; PROTEIN CONFORMATION; ULTRAVIOLET RAYS; VISCOSITY;

BOVINAE;

EID: 0033213896     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(19991001)37:1<116::AID-PROT11>3.0.CO;2-I     Document Type: Article

References (26)

1. Thomas PJ, Qu B-H, Pedersen PL. Defective protein folding as a basis of human disease. TIBS 1995;20:456-459.
2. Kelly JW. Alternative conformation of amyloidogenic proteins govern their behavior. Curr Opin Struct Biol 1996;6:11-17.
3. Perutz MF. Mutations make enzyme polymerize. Nature 1997;385: 773-775.
4. Safar J. The folding intermediate concept of prion protein formation and conformational links to infectivity. In: Prusiner SB, editor. Prions, prions, prions. Berlin: Springer; 1998. p 69-76.
5. Guijarro JI, Sunde M, Jones JA, Campbell ID, Dobson CM. Amyloid fibril formation by an SH3 domain. Proc Natl Acad Sci USA 1998;95:4224-4228.
6. San Biagio PL, Bulone D, Emanuele A, Palma MU. Self assembly of biopolymeric structures below the threshold of random crosslink percolation. Biophysical J 1996;70:494-499.
7. San Biagio PL, Madonia F, Newman J, Palma MU. Sol-sol structural transition of aqueous agarose systems. Biopolymers 1986;25:2255-2269.
8. Leone M, Sciortino F, Migliore M, Fornili SL, Palma-Vittorelli MB. Order parameters of gels and gelation kinetics of aqueous agarose system: relation to the spinodal decomposition of the sol. Biopolymers 1987;26:743-761.
9. Emanuele A, Di Stefano L, Giacomazza D, Trapanese M, Palma-Vittorelli MB, Palma MU. Time-resolved study of network self-organization from a biopolymeric solution. Biopolymers 1991;31: 859-868.
10. Bulone D, San Biagio PL. Mesoscopic gel at low agarose concentration in water: a dynamic light scattering study. Biophys J 1995;68: 1569-1573.
11. San Biagio PL, Palma MU. Spinodal line and Flory-Huggins free energies for solutions of human hemoglobin HbS and HbA. Biophys J 1991;60:508-512.
12. Sciortino F, Prasad KU, Urry DW, Palma MU. Self-assembly of bioelastomeric structures from solutions: mean-field critical behavior and Flory-Huggins free energy of interactions. Biopolymers 1993;33:743-752.
13. Manno M, Emanuele A, Martorana V, et al. Multiple interactions between molecular and supramolecular ordering. Physical Rev E 1999;59:2222-2230.
14. Manno M, Palma MU. Fractal morphology and interacting processes in gelation. Phys Rev Lett 1997;79:4286-4289.
15. Landau LD, Lifshitz EM. Statistical physics. London: Pergamon Press; 1958.
16. Takeda K, Wade A, Yamamoto K, Moriyame Y, Aoki K. Conformational change of bovine serum albumin by heat treatment. J Prot Chem 1989;8:653-659.
17. Venyaminov SY, Yang JT. Determination of protein secondary structure. In: Fasman GD, editor. Theory of circular dichroism and the conformational analysis of biomolecules. New York: Plenum Press; 1996. p 69-107.
18. Woody RW, Dunker AK. Aromatic and cystine side-chain circular dichroism in proteins. In: Fasman GD, editor. Theory of circular dichroism and the conformational analysis of biomolecules. New York: Plenum Press; 1996. p. 109-157.
19. Barone G, Giancola C, Verdoliva A. DSC studies on the denaturation and aggregation of serum albumins. Thermochim Acta 1992;199:197-205.
20. Schmitz KS. An introduction to dynamic light scattering by macromolecules. New York and London: Academic Press; 1990.
21. Flory PJ. Principles of polymer chemistry. London: Cornell University Press; 1953.
22. Emanuele A, Palma-Vittorelli MB. Time-resolved experimental study of shear viscosity in the course of spinodal demixing. Phys Rev Lett 1998;69:81-84.
23. Bulone D, San Biagio PL, Palma-Vittorelli MB, Palma MU. On the role of water in hemoglobin function and stability. Science 1993; 259:1335-1336.
24. Eaton WA, Hofrichter J. Sickle cell hemoglobin polymerization. Adv Prot Chem 1990;40:63-279.
25. San Biagio PL, Bulone D, Martorana V, Palma-Vittorelli MB, Palma MU. Physics and biophysics of solvent induced forces: hydrophobic interactions and context-dependent hydration. Eur Biophys J 1998;27:183-196.
26. Martorana V, Corongiu G, Palma MU. Interaction of explicit solvent with hydrophobic/philic/charged residues of a protein: residue character vs. conformational context. Proteins 1998;32: 129-135.