Α+β protein fold

From Wikipedia, the free encyclopedia

An α+β protein fold is a class of structural domains in which the secondary structure is composed of α-helices and β-strands that occur separately along the backbone. The β-strands are therefore mostly antiparallel.

Common examples include the ferredoxin fold, ribonuclease A, and the SH2 domain.

[edit] See also

• SCOP database
• CATH database
• FSSP database

This protein-related article is a stub. You can help Wikipedia by expanding it.

Retrieved from "http://en.wikipedia.org../../../%CE%B1/%2B/%CE%B2/%CE%91%2B%CE%B2_protein_fold.html"

Categories: Protein stubs | Protein folds

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• This page was last modified 06:34, 13 September 2006 by Wikipedia user Alaibot. Based on work by Wikipedia user(s) WillowW.
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