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| | Ionic Strength Effect on the Thermal Unfolding of -Spectrin Peptides |
 | | Ionic Strength Effect on the Thermal Unfolding of -Spectrin Peptides |
 | | In previous work, we have shown that the ionic strength-mediated differences found for the hydrodynamic dimensions of the human erythrocyte spectrin are not caused by secondary structural changes, but are caused more probably by subtle changes in tertiary interactions (LaBrake, C. C., Wang, L., Keiderling, T. A., and Fung, L. Biochemistry 32, 10296-10302.). |
 | | However, we found that ionic strength-induced cooperativity in the unfolding processes was similar for the spectrin dimer and for peptides with two or three domains, as measured by entropy changes ( |
| pubs.acs.org /cgi-bin/abstract.cgi/bichaw/1998/37/i47/abs/bi9811462.html (273 words) |
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