Kinetics of conformation change of sperm-whale myoglobin. II. Characterization of the rapidly and slowly formed denatured species (D and D*)
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00760a017
Reference9 articles.
1. Helix contents of solutions of native and acid-denatured ferrihemoglobin and ferrimyoglobin
2. Changes in Side Chain Reactivity Accompanying the Binding of Heme to Sperm Whale Apomyoglobin
3. Relative effects of primary and tertiary structure on helix formation in myoglobin and α-lactalbumin
4. Conformation of denatured proteins
5. Die Konformationsänderungen des Pottwal-Metmyoglobins bei der reversiblen Denaturierung im pH-Bereich 7 bis 1
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