Natural polypeptide scaffolds: beta-sheets, beta-turns, and beta-hairpins.
This paper provides an introduction to fundamental conformational states of polypeptides in the beta-region of phi,psi space, in which the backbone is extended near to its maximal length, and to more complex architectures in which extended segments are linked by turns and loops. There are several variants on these conformations, and they comprise versatile scaffolds for presentation of side chains and backbone amides for molecular recognition and designed catalysts. In addition, the geometry of these fundamental folds can be readily mimicked in peptidomimetics.
Rotondi
Kenneth S
KS
Department of Biochemistry and Molecular Biology, University of Massachusetts Amherst, Amherst, MA 01002, USA.
Gierasch
Lila M
LM
D022801:Complementarity Determining Regions / Q000737:chemistry; D008962:Models, Theoretical; D018832:Molecular Chaperones / Q000737:chemistry; D015394:Molecular Structure; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D047011:Silk / Q000737:chemistry
D022801:Complementarity Determining Regions; D018832:Molecular Chaperones; D047011:Silk