The low-pH unfolded state of the C-terminal domain of the ribosomal protein L9 contains significant secondary structure in the absence of denaturant but is no more compact than the low-pH urea unfolded state.

Biochemistry
Bing ShanDaniel P Raleigh

Abstract

There is considerable interest in the properties of the unfolded states of proteins, particularly unfolded states which can be populated in the absence of high concentrations of denaturants. Interest in the unfolded state ensemble reflects the fact that it is the starting point for protein folding as well as the reference state for protein stability studies and can be the starting state for pathological aggregation. The unfolded state of the C-terminal domain (residues 58-149) of the ribosomal protein L9 (CTL9) can be populated in the absence of denaturant at low pH. CTL9 is a 92-residue globular alpha, beta protein. The low-pH unfolded state contains more secondary structure than the low-pH urea unfolded state, but it is not a molten globule. Backbone ( (1)H, (13)C, and (15)N) NMR assignments as well as side chain (13)C beta and (1)H beta assignments and (15)N R 2 values were obtained for the pH 2.0 unfolded form of CTL9 and for the urea unfolded state at pH 2.5. Analysis of the deviations of the chemical shifts from random coil values indicates that residues that comprise the two helices in the native state show a clear preference for adopting helical phi and psi angles in the pH 2.0 unfolded state. There is a less pronounced...Continue Reading

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Citations

Jan 21, 2010·Journal of the American Chemical Society·Jorge Pedro López-AlonsoDouglas V Laurents
Oct 8, 2011·Current Opinion in Structural Biology·Bruce E Bowler
Jun 24, 2015·Nucleic Acids Research·Irina P SuarezRodolfo M Rasia
Oct 27, 2016·Journal of the American Chemical Society·Yi ZhangCatherine A Royer
Jan 5, 2014·Demography·Prashant LoyalkaXiaoying Zheng
Feb 6, 2018·Biophysical Journal·Travis A Danielson, Bruce E Bowler

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