The Effect of pH on the Folding and Stability of the Myosin Rod
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1995.501_b.x/fullpdf
Reference36 articles.
1. Correlation among the proton charges and molecular masses of myosin subunits
2. Magnesium ion dependent adenosine triphosphatase activity of heavy meromyosin as a function of temperature between +20 and -15.degree.C
3. Study of effects of pH on the stability of domains in myosin rod by high-resolution differential scanning calorimetry
4. Hinge region of myosin
5. Tryptophan fluorescence quenching in rabbit skeletal myosin rod
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2. Biochemical and Conformational Changes of Myosin Purified from Pacific Sardine at Various pHs;Journal of Food Science;2008-04
3. Influence of pH on the solubility and conformational characteristics of muscle proteins from mullet (Mugil cephalus);Process Biochemistry;2007-07
4. Solubility Properties of a 65-kDa Peptide Prepared by Restricted Digestion of Myosin with Astacin-like Squid Metalloprotease;Zoological Science;2004-02
5. 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
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