Salts and Glycine Increase Reversibility and Decrease Aggregation during Thermal Unfolding of Ribonuclease-A | Zendy

Yoshiko Kita | Zendy; Tsutomu Arakawa | Zendy

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Salts and Glycine Increase Reversibility and Decrease Aggregation during Thermal Unfolding of Ribonuclease-A

Author(s) -

Yoshiko Kita,

Tsutomu Arakawa

Publication year - 2002

Publication title -

bioscience biotechnology and biochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.509

H-Index - 116

eISSN - 1347-6947

pISSN - 0916-8451

DOI - 10.1271/bbb.66.880

Subject(s) - ribonuclease , rnase p , glycine , chemistry , circular dichroism , folding (dsp implementation) , protein aggregation , ammonium sulfate , protein folding , crystallography , biophysics , chromatography , amino acid , biochemistry , rna , biology , electrical engineering , gene , engineering

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 formation of soluble oligomers. Ammonium sulfate at 0.4 M caused about a 3 degrees C higher melting temperature and nearly complete reversibility, while glycine and NaCl at 0.4 M significantly increased reversibility and decreased aggregation without affecting melting temperature. These results demonstrate that aggregation makes thermal unfolding of RNase-A at least partially irreversible and salts and glycine increase reversibility and decrease aggregation.

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