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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| Published in | Protein science Vol. 11; no. 8; pp. 2048 - 2051 |
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| Main Authors | , |
| Format | Journal Article |
| Language | English |
| Published |
Bristol
Cold Spring Harbor Laboratory Press
01.08.2002
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| Subjects | |
| Online Access | Get full text |
| ISSN | 0961-8368 1469-896X |
| DOI | 10.1110/ps.0211702 |
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| 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. |
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| AbstractList | 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. 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.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. |
| Author | Celinski, Scott A. Scholtz, J. Martin |
| AuthorAffiliation | Department of Medical Biochemistry & Genetics, Department of Biochemistry & Biophysics, Center for Advanced Biomolecular Research, Texas A&M University, College Station, Texas 77843-1114, USA |
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| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/12142459$$D View this record in MEDLINE/PubMed |
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| Cites_doi | 10.1016/0076-6879(86)31045-0 10.1021/bi960341i 10.1021/ja00013a079 10.1126/science.7112124 10.1021/bi00088a019 10.1021/bi970247h 10.1073/pnas.92.1.185 10.1073/pnas.95.16.9268 10.1002/pro.5560030514 10.1006/jmbi.2001.4819 10.1021/bi002078y 10.1016/S0065-3233(08)60334-4 10.1016/B978-012310920-0/50005-X 10.1021/bi00039a051 10.1063/1.1730390 10.1146/annurev.bb.22.060193.000435 10.1074/jbc.273.9.4831 10.1063/1.1731802 10.1016/S0021-9258(19)68947-7 10.1093/oso/9780199636198.003.0012 10.1042/bj1830317 10.1006/jmbi.2000.3936 10.1021/bi00459a037 |
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| Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 Article and publication are at http://www.proteinscience.org/cgi/doi/10.1110/ps.0211702. Reprint requests to: J. Martin Scholtz, Department of Medical Biochemistry & Genetics, Department of Biochemistry & Biophysics, Center for Advanced Biomolecular Research, Texas A&M University, College Station, TX 77843-1114, USA; e-mail: jm-scholtz@tamu.edu; fax: 979-847 9481. |
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| SubjectTerms | 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 |
| Title | Osmolyte effects on helix formation in peptides and the stability of coiled‐coils |
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