Abstract
Protein refolding from unfolded state is usually carried out at low temperature to reduce protein aggregation and proteolytic degradation. This review briefly introduces a unique method for the protein refolding via high temperature, typically at above melting temperature of the protein.
Keywords: Inclusion bodies, protein refolding
Current Pharmaceutical Biotechnology
Title: Thermal-Assisted Refolding: Dilution Folding Initiated at High Temperature
Volume: 11 Issue: 3
Author(s): Kentaro Shiraki and Soichiro Kayano
Affiliation:
Keywords: Inclusion bodies, protein refolding
Abstract: Protein refolding from unfolded state is usually carried out at low temperature to reduce protein aggregation and proteolytic degradation. This review briefly introduces a unique method for the protein refolding via high temperature, typically at above melting temperature of the protein.
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Cite this article as:
Shiraki Kentaro and Kayano Soichiro, Thermal-Assisted Refolding: Dilution Folding Initiated at High Temperature, Current Pharmaceutical Biotechnology 2010; 11 (3) . https://dx.doi.org/10.2174/138920110791111988
DOI https://dx.doi.org/10.2174/138920110791111988 |
Print ISSN 1389-2010 |
Publisher Name Bentham Science Publisher |
Online ISSN 1873-4316 |
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