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Side‐chain control of β‐peptide secondary structures : Design principles: Design principles
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| Zeitschriftentitel: | European Journal of Biochemistry |
|---|---|
| Personen und Körperschaften: | , |
| In: | European Journal of Biochemistry, 270, 2003, 18, S. 3657-3666 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Wiley
|
| Schlagwörter: |
| author_facet |
Martinek, Tamás A. Fülöp, Ferenc Martinek, Tamás A. Fülöp, Ferenc |
|---|---|
| author |
Martinek, Tamás A. Fülöp, Ferenc |
| spellingShingle |
Martinek, Tamás A. Fülöp, Ferenc European Journal of Biochemistry Side‐chain control of β‐peptide secondary structures : Design principles Biochemistry |
| author_sort |
martinek, tamás a. |
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Martinek, Tamás A. Fülöp, Ferenc 0014-2956 1432-1033 Wiley Biochemistry http://dx.doi.org/10.1046/j.1432-1033.2003.03756.x <jats:p>As one of the most important families of non‐natural polymers with the propensity to form well‐defined secondary structures, the β‐peptides are attracting increasing attention. The compounds incorporating β‐amino acid residues have found various applications in medicinal chemistry and biochemistry. The conformational pool of β‐peptides comprises several periodic folded conformations, which can be classified as helices, and nonpolar and polar strands. The latter two are prone to form pleated sheets. The numerous studies that have been performed on the side‐chain dependence of the stability of the folded structures allow certain conclusions concerning the principles of design of the β‐peptide foldamers. The folding propensity is influenced by local torsional, side‐chain to backbone and long‐range side‐chain interactions. Although β‐peptide foldamers are sensitive to solvent, the systematic choice of the side‐chain pattern and spatiality allows the design of the desired specific secondary structure. The application of β‐peptide foldamers may open up new directions in the synthesis of highly organized artificial tertiary structures with biochemical functions.</jats:p> Design principles Side‐chain control of β‐peptide secondary structures : Design principles European Journal of Biochemistry |
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Design principles |
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Side‐chain control of β‐peptide secondary structures : Design principles |
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Side‐chain control of β‐peptide secondary structures : Design principles |
| title_full |
Side‐chain control of β‐peptide secondary structures : Design principles |
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Side‐chain control of β‐peptide secondary structures : Design principles |
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Side‐chain control of β‐peptide secondary structures : Design principles |
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Side‐chain control of β‐peptide secondary structures : Design principles |
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side‐chain control of β‐peptide secondary structures : design principles |
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Biochemistry |
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http://dx.doi.org/10.1046/j.1432-1033.2003.03756.x |
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2003 |
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3657-3666 |
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<jats:p>As one of the most important families of non‐natural polymers with the propensity to form well‐defined secondary structures, the β‐peptides are attracting increasing attention. The compounds incorporating β‐amino acid residues have found various applications in medicinal chemistry and biochemistry. The conformational pool of β‐peptides comprises several periodic folded conformations, which can be classified as helices, and nonpolar and polar strands. The latter two are prone to form pleated sheets. The numerous studies that have been performed on the side‐chain dependence of the stability of the folded structures allow certain conclusions concerning the principles of design of the β‐peptide foldamers. The folding propensity is influenced by local torsional, side‐chain to backbone and long‐range side‐chain interactions. Although β‐peptide foldamers are sensitive to solvent, the systematic choice of the side‐chain pattern and spatiality allows the design of the desired specific secondary structure. The application of β‐peptide foldamers may open up new directions in the synthesis of highly organized artificial tertiary structures with biochemical functions.</jats:p> |
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| description | <jats:p>As one of the most important families of non‐natural polymers with the propensity to form well‐defined secondary structures, the β‐peptides are attracting increasing attention. The compounds incorporating β‐amino acid residues have found various applications in medicinal chemistry and biochemistry. The conformational pool of β‐peptides comprises several periodic folded conformations, which can be classified as helices, and nonpolar and polar strands. The latter two are prone to form pleated sheets. The numerous studies that have been performed on the side‐chain dependence of the stability of the folded structures allow certain conclusions concerning the principles of design of the β‐peptide foldamers. The folding propensity is influenced by local torsional, side‐chain to backbone and long‐range side‐chain interactions. Although β‐peptide foldamers are sensitive to solvent, the systematic choice of the side‐chain pattern and spatiality allows the design of the desired specific secondary structure. The application of β‐peptide foldamers may open up new directions in the synthesis of highly organized artificial tertiary structures with biochemical functions.</jats:p> |
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| spelling | Martinek, Tamás A. Fülöp, Ferenc 0014-2956 1432-1033 Wiley Biochemistry http://dx.doi.org/10.1046/j.1432-1033.2003.03756.x <jats:p>As one of the most important families of non‐natural polymers with the propensity to form well‐defined secondary structures, the β‐peptides are attracting increasing attention. The compounds incorporating β‐amino acid residues have found various applications in medicinal chemistry and biochemistry. The conformational pool of β‐peptides comprises several periodic folded conformations, which can be classified as helices, and nonpolar and polar strands. The latter two are prone to form pleated sheets. The numerous studies that have been performed on the side‐chain dependence of the stability of the folded structures allow certain conclusions concerning the principles of design of the β‐peptide foldamers. The folding propensity is influenced by local torsional, side‐chain to backbone and long‐range side‐chain interactions. Although β‐peptide foldamers are sensitive to solvent, the systematic choice of the side‐chain pattern and spatiality allows the design of the desired specific secondary structure. The application of β‐peptide foldamers may open up new directions in the synthesis of highly organized artificial tertiary structures with biochemical functions.</jats:p> Design principles Side‐chain control of β‐peptide secondary structures : Design principles European Journal of Biochemistry |
| spellingShingle | Martinek, Tamás A., Fülöp, Ferenc, European Journal of Biochemistry, Side‐chain control of β‐peptide secondary structures : Design principles, Biochemistry |
| title | Side‐chain control of β‐peptide secondary structures : Design principles |
| title_full | Side‐chain control of β‐peptide secondary structures : Design principles |
| title_fullStr | Side‐chain control of β‐peptide secondary structures : Design principles |
| title_full_unstemmed | Side‐chain control of β‐peptide secondary structures : Design principles |
| title_short | Side‐chain control of β‐peptide secondary structures : Design principles |
| title_sort | side‐chain control of β‐peptide secondary structures : design principles |
| title_sub | Design principles |
| title_unstemmed | Side‐chain control of β‐peptide secondary structures : Design principles |
| topic | Biochemistry |
| url | http://dx.doi.org/10.1046/j.1432-1033.2003.03756.x |