Osmolyte effects on helix formation in peptides and the stability of coiled‐coils

The ability of several naturally occurring substances known as osmolytes to induce helix formation in an alanine‐based peptide have been investigated. As predicted by the osmophobic effect hypothesis, the osmolytes studies here do induce helix formation. Trimethylamine‐N‐oxide (TMAO) is the best str...

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Bibliographic Details
Published in:Protein science 2002-08, Vol.11 (8), p.2048-2051
Main Authors: Celinski, Scott A., Scholtz, J. Martin
Format: Article
Language:English
Subjects:
Alanine - chemistry
Amino Acid Sequence
Circular Dichroism
Dimerization
DNA-Binding Proteins
For the Record
helix‐coil transition
leucine zipper
Leucine Zippers - drug effects
Methylamines - pharmacology
Molecular Sequence Data
Osmolar Concentration
peptide stability
Protein Denaturation
Protein Folding
Protein Kinases - chemistry
Protein Structure, Secondary - drug effects
Saccharomyces cerevisiae Proteins - chemistry
TFE, 1,1,1‐trifluoroethanol
TMAO
TMAO, trimethylamine N‐oxide
Trifluoroethanol - pharmacology
Urea - pharmacology
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Summary:The ability of several naturally occurring substances known as osmolytes to induce helix formation in an alanine‐based peptide have been investigated. As predicted by the osmophobic effect hypothesis, the osmolytes studies here do induce helix formation. Trimethylamine‐N‐oxide (TMAO) is the best structure‐inducing osmolytes investigated here, but it is not as effective in promoting helix formation as the common cosolvent trifluoroethanol (TFE). We also provide a semiquantitative study of the ability of TMAO to induce helix formation and urea, which acts as a helix (and protein) denaturant. We find that on a molar basis, these agents are exactly counteractive as structure inducing and unfolding agents. Finally, we extend the investigations to the effects of urea and TMAO on the stability of a dimeric coiled‐coil peptide and find identical results. Together these results support the tenets of the osmophobic hypothesis and highlight the importance of the polypeptide backbone in protein folding and stability.
ISSN:0961-8368
1469-896X
DOI:10.1110/ps.0211702