Mechanism of phage P22 tailspike protein folding mutations
Author:
Publisher
Wiley
Subject
Molecular Biology,Biochemistry
Reference41 articles.
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3. Kinetic characterization of early immunoreactive intermediates during the refolding of guanidine-unfolded Escherichia coli tryptophan syntase β2 subunits;Blond-Elguindi;Biochemistry,1990
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2. Bacteriophage P22 tailspike: structure of the complete protein and function of the interdomain linker;Acta Crystallographica Section D Biological Crystallography;2014-04-30
3. The C-terminus of the P22 tailspike protein acts as an independent oligomerization domain for monomeric proteins;Biochemical Journal;2009-04-14
4. Multimeric intermediates in the pathway to the aggregated inclusion body state for P22 tailspike polypeptide chains;Protein Science;2008-12-31
5. Folding and Association of Multi-domain and Oligomeric;Protein Science Encyclopedia;2008-03-15
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