Apomyoglobin folding intermediates characterized by the hydrophobic fluorescent probe 8-anilino-1-naphthalene sulfonate (ANS)
- 26 June 1998
- journal article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
- Vol. 1385 (1) , 69-77
- https://doi.org/10.1016/s0167-4838(98)00038-7
Abstract
No abstract availableKeywords
This publication has 48 references indexed in Scilit:
- Thermodynamic Stability of the Molten Globule States of ApomyoglobinJournal of Molecular Biology, 1995
- Unfolding Pathway of ApomyoglobinJournal of Molecular Biology, 1994
- Molecular Mechanisms of Acid DenaturationJournal of Molecular Biology, 1994
- The molten globule is a third thermodynamical state of protein moleculesFEBS Letters, 1994
- Structure and dynamics of the acidic compact state of apomyoglobin by frequency‐domain fluorometryEuropean Journal of Biochemistry, 1993
- Phase diagram for acidic conformational states of apomyoglobinJournal of Molecular Biology, 1990
- Thermodynamic study of the apomyoglobin structureJournal of Molecular Biology, 1988
- ‘Molten‐globule state’: a compact form of globular proteins with mobile side‐chainsFEBS Letters, 1983
- The interaction of a naphthalene dye with apomyoglobin and apohemoglobinJournal of Molecular Biology, 1965
- Cleavage of the haem-protein link by acid methylethylketoneBiochimica et Biophysica Acta, 1959