Thermal Aggregation of Ribonuclease A
نویسندگان
چکیده
منابع مشابه
Salts and glycine increase reversibility and decrease aggregation during thermal unfolding of ribonuclease-A.
Ribonuclease-A (RNase-A) has been a model for studying protein folding and unfolding. However, we show here that its unfolding at neutral pH is complicated by aggregation. Circular dichroism thermal scans showed that reversibility of RNase-A after heating is only about 63%. In accordance with this observation, native-polyacrylamide gel electrophoresis of the sample heated at 75 degrees C showed...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2003
ISSN: 0021-9258
DOI: 10.1074/jbc.m213146200