Immunological measurements of conformational motility in regions of the myoglobin molecule (original) (raw)

The conformational motilities of three regions of the sperm whale myoglobin molecule and of an isolated peptide of myoglobin have been examined by measuring the equilibrium constant for the nativenonnative transition. The immunological approach of Furie et al. (Furie, B., Schechter, A. N., Sachs, D., and Anfinsen, C. B. (1 975), J . Mol. Biol. 92, [497][498][499][500][501][502][503][504][505][506] was used with convenient modifications. Antibodies specific to the nonnative conformations were used in assaying for competition between the radioactively labeled peptide and native myoglobin. Labeling was by lZsI iodination of the peptide or its 3-(4-hydroxyphenyl)propionyl derivative, and sep-G l o b u l a r proteins in solution undergo conformational fluctuations during which their structure alternates rapidly between native and nonnative conformations (Anfinsen and Scheraga, 1975). The native structure, which normally predominates, is in equilibrium with a population of nonnative or "denatured" states that are present in concentrations below the limit of detection of physiochemical techniques.

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