α-Helical coiled coils and bundles: How to design an α-helical protein
The presence of a periodic disposition of apolar residues at positions a and d within a heptad repeat (of the form (a b c d e f g) sub(n) super(10)), signals the potential for the interlocking of groups of alpha -helices. This type of periodicity is common in fibrous proteins, is characteristic of m...
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Veröffentlicht in: | Proteins, structure, function, and bioinformatics structure, function, and bioinformatics, 1990, Vol.7 (1), p.1-15 |
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Hauptverfasser: | , |
Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | The presence of a periodic disposition of apolar residues at positions a and d within a heptad repeat (of the form (a b c d e f g) sub(n) super(10)), signals the potential for the interlocking of groups of alpha -helices. This type of periodicity is common in fibrous proteins, is characteristic of most membrane proteins, and is found as well in a wide range of globular proteins. Here the structures of these three protein classes are related more closely and special features of design are noted. |
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ISSN: | 0887-3585 1097-0134 |
DOI: | 10.1002/prot.340070102 |