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Anfinsen

Anfinsen C B 1973 Prinoiples that govern the folding of protein ohains Science 181 223-30... [Pg.2664]

CB Anfinsen. Principles that govern the folding of protein chains. Science 181 223-238, 1973. [Pg.308]

C. B. Anfinsen (Bethesda) work on ribo-nuclease, especially concerning the connection between the amino-acid sequence and the biologically active conformation. [Pg.1298]

Anfinsen s thermodynamic hypothesis, which states that the native state for a protein in its physiological milieu is the one of lowest Gibbs free energy (Anfinsen, 1973). [Pg.16]

Staphylococcal nuclease is a small a + ft protein of 149 amino acids that is stable to denaturation by only +5.5 kcal/mol (Anfinsen et al.,... [Pg.27]

Anfinsen, C. B., Schecter, A. N., andTaniuchi, H. (1972). Cold Spring Harbor Symp. Quant. Biol. 36, 249-255. [Pg.45]

Christianson D (1991) Structural biology of zinc. In Anfinsen C, Richards F, Edsall J, Eisenberg D (eds) Advances in protein chemistry. Metalloproteins structural aspects, vol 42. Academic Press, p 281... [Pg.166]

Goldberg, R. F., Epstein, C.)., Anfinsen, C. B., Acceleration of reactivation of reduced bovine pancreatic ribonuclease by a microsomal system from rat liver, /. Biol. Chem. 238 (1963), p. 628-635... [Pg.104]

In summary, the physiological control of silk protein conversion shows an ingenious balance of activating and inhibiting mechanisms that are dependent on composition and sequence arrangement (Krejchi et al., 1994). Denaturing effects observed in silks appear to be identical to those found in amyloid-forming proteins, and they principally alter the competitive outcome of the hydration of nonpolar and polar residues (Anfinsen, 1973 Dill, 1990 Dobson and Karplus, 1999 Kauzmann, 1959). The key differences to amyloids may lie in the hierarchical level of the structures (Muthukumar et al., 1997) involved in the assembly of silks compared to amyloids. [Pg.37]

The forces that stabilize amyloid fibrils include specific hydrogen bonding, electrostatic interactions, n-n stacking, and hydrophobic interactions. Importantly, similar types of interactions stabilize the functional native structures of protein molecules (Anfinsen, 1973 Dill, 1990 Dobson and Karplus, 1999 Kauzmann, 1959). In this sense, the conditions that favor native protein folding might also be manipulated to facilitate the formation of amyloid fibrils. [Pg.39]

M Ohno, CB Anfinsen. Removal of protected peptides by hydrazinolysis after synthesis by solid-phase. J Am Chem Soc 89, 5994, 1967. [Pg.226]


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See also in sourсe #XX -- [ Pg.245 ]

See also in sourсe #XX -- [ Pg.33 , Pg.95 ]




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