Macromolecular Crowding Stabilizes the Molten Globule Form of Apomyoglobin with Respect to Both Cold and Heat Unfolding
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Structural Biology
Reference12 articles.
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3. Effects of macromolecular crowding on the unfolding and the refolding of D-glyceraldehyde 3-phosphate dehydrogenase;Ren;J. Protein Chem.,2003
4. Cold denaturation of the molten globule states of apomyoglobin and a profile for protein folding;Nishii;Biochemistry,1994
5. Comparison of myoglobins from harbour seal, porpoise and sperm whale. I. Preparation and characterisation;Hapner;J. Biol. Chem.,1968
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