منابع مشابه
Reconstitution of Acid-denatured Catalase.
The current interest in the reversibility of protein denaturation is prompted by the idea that, unlike the amino acid sequence, the secondary, tertiary, and quaternary structures of native protein molecules may not be genetically predetermined during biosynthesis. If this viewpoint is correct, unfolded polypeptide chains, on denaturation of proteins, should be able under favorable conditions to...
متن کاملStructure and dynamics of an acid-denatured protein G mutant.
NMR studies of protein denatured states provide insights into potential initiation sites for folding that may be too transient to be observed kinetically. We have characterized the structure and dynamics of the acid-denatured state of protein G by using a F30H mutant of G(B1) which is on the margin of stability. At 5 degrees C, F30H-G(B1) is greater than 95% folded at pH 7.0 and is greater than...
متن کاملProduction of Antibodies to Denatured Deoxyribonucleic Acid (dna).
* This work was supported by grant 23571 of the National Science Foundation, and grant AI04865-02 from the National Institutes of Health. Mortenson, L. E., Ann. Rev. Microbiol., 17, 115 (1963). 2 Mortenson, L. E., Biochim. Biophys. Acta, 81, 473 (1964). 3 Wilson, P. W., in Handbuch der P;flanzenphysiologie, ed. W. Ruhland (Berlin: Springer, 1958), vol. 8, p. 9. 4 McNary, J. E., and R. H. Burris...
متن کاملSolvent-induced collapse of -synuclein and acid-denatured cytochrome c
The effects of solution conditions on protein collapse were studied by measuring the hydrodynamic radii of two unfolded proteins, -synuclein and acid-denatured ferricytochrome c, in dilute solution and in 1 M glucose. The radius of -synuclein in dilute solution is less than that predicted for a highly denatured state, and adding 1 M glucose causes further collapse. Circular dichroic data show t...
متن کاملEvidence for residual structure in acid- and heat-denatured proteins.
A number of very careful studies have been made in recent years of the thermal transitions which small globular proteins undergo at low pH. These transitions reflect the destruction of the ordered conformation of the native protein, and the products of the transition have the properties of highly disordered polypeptide chains. The principal objective of such studies has, however, been to determ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1963
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)48655-3