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Protein Science, Vol 6, Issue 12 2578-2588, Copyright © 1997 by Cold Spring Harbor Laboratory Press

ARTICLE

Lack of coupling between secondary structure formation and collapse in a model polypeptide that mimics early folding intermediates, the F(2) fragment of the Escherichia coli tryptophan-synthase {beta} chain

K. GAST, A. F. CHAFFOTTE, D. ZIRWER, Y. GUILLOU, M. MUELLER-FROHNE, C. CADIEUX, M. HODGES, G. DAMASCHUN and M. E. GOLDBERG
Max Delbruck Center for Molecular Medicine, Robert-Rossle Str. 10, D 13122 Berlin, Germany

The isolated, 101-residue long C-terminal (so called F(2)) fragment of the {beta} chain from Escherichia coli tryptophan synthase was shown previously to fold into an ensemble of conformations that are condensed, to contain large amounts of highly dynamic secondary structures, and to behave as a good model of structured intermediates that form at the very early stages of protein folding. Here, solvent perturbations were used to investigate the forces that are involved in stabilizing the secondary structure (monitored by far-UV CD) and the condensation of the polypeptide chain (monitored by dynamic light scattering) in isolated F(2). It was observed that neither the ionic strength, nor the pH (between 7 and 10), nor salts of the Hofmeister series affected the global secondary structure contents of F(2), whereas some of these salts affected the collapse slightly. Addition of trifluoroethanol resulted in a large increase in both the amount of secondary structure and the Stokes radius of F(2). Conversely, F(2) became more condensed upon raising the temperature from 4 to 60{deg}C, whereas in this temperature range, the secondary structure undergoes significant melting. These observations lead to the conclusion that, in isolated F(2), there is no coupling between the hydrophobic collapse and the secondary structure. This finding will be discussed in terms of early events in protein folding.
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