The influence of putrescine on the structure, enzyme activity and stability of α-chymotrypsin
Author:
Affiliation:
1. Department of Biology
2. Faculty of Science
3. University of Shahrekord
4. Shahrekord
5. Iran
6. Institute of Biochemistry and Biophysics
7. University of Tehran
8. Tehran
9. Center of Excellence in Biothermodynamics
Abstract
Information on protein stability is essential to study protein structure, activity, and interactions with ligands.
Publisher
Royal Society of Chemistry (RSC)
Subject
General Chemical Engineering,General Chemistry
Link
http://pubs.rsc.org/en/content/articlepdf/2016/RA/C5RA25053F
Reference57 articles.
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4. Effect of polyamines on the structure, thermal stability and 2,2,2-trifluoroethanol-induced aggregation of α-chymotrypsin
5. K. Igarashi , Y.Terui and K.Kashiwagi, in Polyamines, Springer, 2015, pp. 131–141
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