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Circular Permutation of a Chaperonin Protein: Biophysics and Application to NanotechnologyWe have designed five circular permutants of a chaperonin protein derived from the hyperthermophilic organism Sulfolobus shibatae. These permuted proteins were expressed in E. coli and are well-folded. Furthermore, all the permutants assemble into 18-mer double rings of the same form as the wild-type protein. We characterized the thermodynamics of folding for each permutant by both guanidine denaturation and differential scanning calorimetry. We also examined the assembly of chaperonin rings into higher order structures that may be used as nanoscale templates. The results show that circular permutation can be used to tune the thermodynamic properties of a protein template as well as facilitating the fusion of peptides, binding proteins or enzymes onto nanostructured templates.
Document ID
20050158739
Document Type
Conference Paper
Authors
Paavola, Chad (NASA Ames Research Center Moffett Field, CA, United States)
Chan, Suzanne (Search for Extraterrestrial Intelligence Inst. CA, United States)
Li, Yi-Fen (Search for Extraterrestrial Intelligence Inst. CA, United States)
McMillan, R. Andrew (NASA Ames Research Center Moffett Field, CA, United States)
Trent, Jonathan (NASA Ames Research Center Moffett Field, CA, United States)
Date Acquired
August 23, 2013
Publication Date
January 1, 2004
Subject Category
Life Sciences (General)
Meeting Information
18th Symposium of the Protein Society Protein Structure, Function and Disease(La Jolla, CA)
Funding Number(s)
OTHER: 302-05-46
Distribution Limits
Public
Copyright
Work of the US Gov. Public Use Permitted.