Journal article
Osmolyte effects on helix formation in peptides and the stability of coiled-coils
Protein science, Vol.11(8), pp.2048-2051
08/2002
DOI: 10.1110/ps.0211702
PMCID: PMC2373673
PMID: 12142459
Abstract
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.
Details
- Title: Subtitle
- Osmolyte effects on helix formation in peptides and the stability of coiled-coils
- Creators
- Scott A Celinski - Texas A&M UniversityJ Martin Scholtz - Texas A&M University
- Resource Type
- Journal article
- Publication Details
- Protein science, Vol.11(8), pp.2048-2051
- DOI
- 10.1110/ps.0211702
- PMID
- 12142459
- PMCID
- PMC2373673
- NLM abbreviation
- Protein Sci
- ISSN
- 0961-8368
- eISSN
- 1469-896X
- Grant note
- R29 GM052483 / NIGMS NIH HHS GM-52483 / NIGMS NIH HHS R01 GM052483 / NIGMS NIH HHS
- Language
- English
- Date published
- 08/2002
- Academic Unit
- Research Administration; Pharmaceutical Sciences and Experimental Therapeutics; Biochemistry and Molecular Biology; Chemistry
- Record Identifier
- 9984288726002771
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