Accessibility of folding mutation sites in the native phage p22 tailspike protein trimer

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Title
Accessibility of folding mutation sites in the native phage p22 tailspike protein trimer
Author(s)
M BeiBinger; Myeong Hee Yu; R Seckler
Bibliographic Citation
Protein and Peptide Letters, vol. 1, no. 1, pp. 1-4
Publication Year
1994
Abstract
Cystein substitutions at sites of 3 temperature-sensitive-folding (tsf) and 2 tsf-suppressor mutations in the phage P22 tailspike protein were created in order to probe the solvent accessibility of these sites. Cysteines at 2 tsf sites (residues 235 and 244) reacted readily with Ellman's reagent and labeled by fluorescent maleimides. Spectra of the labeled proteins indicated the electrostatic enviornment of the 2 sites to be different. The 2 suppressor sites (residues 331 and 334) and residue 238 were inaccessible to the reagents.
ISSN
0929-8665
Publisher
Bentham Science Publ Ltd
Type
Article
Appears in Collections:
1. Journal Articles > Journal Articles
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