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Structural Evidence for a Possible Role of Reversible Disulphide Bridge Formation in the Elasticity of the Muscle Protein Titin

✍ Scribed by Olga Mayans; Jochen Wuerges; Santiago Canela; Mathias Gautel; Matthias Wilmanns

Book ID
114328923
Publisher
Elsevier Science
Year
2001
Tongue
English
Weight
890 KB
Volume
9
Category
Article
ISSN
0969-2126

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Isolation of several of the charge isomers from both normal and multiple sclerosis (MS) myelin basic protein (MBP) was achieved on CM-52 columns at pH 10.6. In liquid x-ray diffraction and aggregation experiments, corresponding charge isomers were equally effective in the formation of multilayers, d