NDLI: Conformational Behavior of Chemically Reactive Alanine-Rich Repetitive Protein Polymers

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Conformational Behavior of Chemically Reactive Alanine-Rich Repetitive Protein Polymers

Content Provider	PubMed Central
Author	Farmer, Robin S. Kiick, Kristi L.
Abstract	The synthesis of protein-based polymers with controlled conformational properties and functional group placement offers many opportunities for the design of advanced materials. In this work, protein engineering methods have been used to produce repetitive alanine-rich protein polymers with the sequence [(AAAQ)5-(AAAE)(AAAQ)5] x (x = 2 and 6); these macromolecules may mimic architectural features of certain alanine-rich helical sequences found in natural proteins. Various proteins from this family can be readily expressed and purified from Escherichia coli. Circular dichroic spectroscopy (CD) characterization demonstrates that the purified proteins are highly helical under a variety of conditions. Thermal analysis of [(AAAQ)5(AAAE)-(AAAQ)5]2 via differential scanning calorimetry (DSC) and CD indicates that the protein undergoes a reversible helix–coil transition at approximately 45 °C and that the protein conformation can be manipulated at elevated temperatures depending on solution conditions. The demonstrated conformational properties of these artificial proteins suggest that they may be excellent candidates for elucidating structure–function relationships in biopolymers for nanotechnology and biological applications.
Related Links	http://dx.doi.org/10.1021/bm049216
Starting Page	1531
File Format	PDF
ISSN	15264602
e-ISSN	15264602
Journal	Biomacromolecules
Issue Number	3
Volume Number	6
Language	English
Publisher Date	2005-01-01
Access Restriction	Open
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Materials Chemistry Biomaterials Bioengineering Polymers and Plastics

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