Unfolding/refolding studies of the myosin rod
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1993.tb18464.x/fullpdf
Reference41 articles.
1. An Electrophoretic Study of Native Myosin Isozymes and of Their Subunit Content
2. Expression in Escherichia coli of fragments of the coiled-coil rod domain of rabbit myosin: influence of different regions of the molecule on aggregation and paracrystal formation
3. Magnesium ion dependent adenosine triphosphatase activity of heavy meromyosin as a function of temperature between +20 and -15.degree.C
4. Study of effects of pH on the stability of domains in myosin rod by high-resolution differential scanning calorimetry
5. α-Helical coiled coils and bundles: How to design an α-helical protein
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1. Physicochemical properties of thiol proteinase inhibitor isolated from goat pancreas;Biopolymers;2010
2. Changes in Conformation and Subunit Assembly of Cod Myosin at Low and High pH and after Subsequent Refolding;Journal of Agricultural and Food Chemistry;2003-10-18
3. Dimerization of the Head–Rod Junction of Scallop Myosin;Biochemical and Biophysical Research Communications;1998-11
4. Unfolding domains and tryptophan accessibility of a 59 kda coiled-coil light meromyosin;Journal of Molecular Biology;1998-03
5. Two-State Thermal Unfolding of a Long Dimeric Coiled-Coil: The Acanthamoeba Myosin II Rod;Biochemistry;1997-06-01
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