Lack of coupling between secondary structure formation and collapse in a model polypeptide that mimics early folding intermediates, the F2 fragment of the Escherichia coli tryptophan-synthase β chain-Reference-Cited by-同舟云学术

Lack of coupling between secondary structure formation and collapse in a model polypeptide that mimics early folding intermediates, the F2 fragment of the Escherichia coli tryptophan-synthase β chain

Published:2008-12-31 Issue:12 Volume:6 Page:2578-2588
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Science

Author:

Gast Klaus,Mueller-Frohne Marlies,Chaffotte Alain F.,Guillou Yvonne,Hodges Maria,Cadieux CÉLine,Goldberg Michel E.,Zirwer Dietrich,Damaschun Gregor

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

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4. A possible initial folding intermediate: The C-terminal proteolytic domain of tryptophan synthase β chains folds in less than 4 milliseconds into a condensed state with non-native-like secondary structure;Chaffotte;Biochemistry,1992a

5. The isolated C-terminal (F2) fragment of the Escherichia coli tryptophan synthase β2-subunit folds into a stable, organized, nonnative conformation;Chaffotte;Biochemistry,1991

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