PMID: 3607240Jul 1, 1987Paper

Thermodynamics of alligator metmyoglobin unfolding

Biophysical Chemistry
L Kelly, L A Holladay

Abstract

The conformational free energy of alligator metmyoglobin was examined over a pH range of 4.4-8.0, a temperature range of 18-48 degrees C, and a guanidinium chloride concentration of 0-2.3 M. For isothermal unfolding at 25 degrees C essentially the same value was obtained for the conformational free energy from all the data: 7.0 +/- 0.5 kcal/mol. The cooperativity of the unfolding with respect to denaturant is considerably less than for mammalian myoglobins. On unfolding three to four side chains with a pKa of 6.3 in the unfolded protein are protonated instead of the six expected. The temperature at which delta H (unfolding) is zero is much lower than for previously characterized myoglobins. Alligator metmyoglobin, considerably less stable than other previously characterized myoglobins, may not be as compactly folded.

References

Mar 5, 1986·Journal of Molecular Biology·G De SanctisM Brunori
Oct 1, 1985·Biophysical Chemistry·L A Holladay
Jul 5, 1974·Journal of Molecular Biology·P L Privalov, N N Khechinashvili
Jan 1, 1972·Methods in Enzymology·K WeberM Osborn
Aug 14, 1968·Journal of Molecular Biology·A N Schechter, C J Epstein
Mar 29, 1967·Journal of the American Chemical Society·G Acampora, J Hermans
Aug 30, 1983·Biochemistry·E BismutoG Irace
Aug 21, 1980·Biochimica Et Biophysica Acta·H DeneA E Romero-Herrera

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Citations

Mar 1, 1990·International Journal of Peptide and Protein Research·L Kelly, L A Holladay
Mar 1, 1988·International Journal of Peptide and Protein Research·L KellyL A Holladay

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