NDLI: Thermal analysis of protein–metallic ion systems

Content Provider	Springer Nature Link
Author	Hu, Xiao Kaplan, David Cebe, Peggy
Copyright Year	2009
Abstract	Advanced thermal analysis methods, such as temperature modulated DSC (differential scanning calorimetry) and quasi-isothermal TMDSC were used to analyze the protein–metallic ion interactions in silk fibroin proteins. The precise heat capacities were measured and theoretically predicted in this study. To remove bound water and simplify the system, a thermal cycling treatment through both standard DSC and TMDSC was used to detect the underlying heat capacity and reveal the phase transitions of the silk–metallic salts system. Results show that K$^{+}$ metallic salts play the role of plasticizer in silk fibroin proteins, which reduces the glass transition (T$_{g}$) of the pure silk protein and negatively affects its structural thermal stability. On the other hand, Ca$^{2+}$ metallic salts act as an anti-plasticizer, and increase the glass transition and the thermal stability of the silk protein structure. This indicates that the thermal analysis methods offer a new pathway to study protein–metallic ion systems, yielding very fruitful information for the study of protein structures in the future.
Starting Page	827
Ending Page	834
Page Count	8
File Format	PDF
ISSN	13886150
Journal	Journal of thermal analysis
Volume Number	96
Issue Number	3
e-ISSN	15728943
Language	English
Publisher	Springer Netherlands
Publisher Date	2009-07-03
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Anti-plasticizer Beta pleated sheets crystal Bombyx mori silk fibroin Differential scanning calorimetry Heat capacity Metal ion Measurement Science, Instrumentation Inorganic Chemistry Polymer Sciences Analytical Chemistry Physical Chemistry
Content Type	Text
Resource Type	Article
Subject	Physical and Theoretical Chemistry Condensed Matter Physics

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